bims-auttor Biomed News
on Autophagy and mTOR
Issue of 2026–10–18
34 papers selected by
Viktor Korolchuk, Newcastle University



  1. Adv Biol Regul. 2026 Oct 07. pii: S2212-4926(26)00043-6. [Epub ahead of print] 101186
      Mitophagy is a form of selective autophagy in which an isolation membrane (IM or phagophore) sequesters damaged or superfluous mitochondria for lysosomal degradation. Recent advances in receptor-mediated mitophagy, particularly the BNIP3/NIX-mediated mitophagy, have highlighted the importance of this pathway in mitochondrial regulation across various biological settings, along with the well-established Parkin-mediated pathway. Parkin-mediated mitophagy senses mitochondrial damage through loss of membrane potential, whereas BNIP3/NIX-mediated mitophagy plays an important role in basal or physiologically induced mitochondrial turnover, thereby contributing to mitochondrial quality control and remodeling. These two pathways employ distinct sets of molecules to recruit the autophagy machinery to the mitochondria and exhibit different IM dynamics that are closely linked to mitochondrial fission and segregation. In this review, we first provide an updated overview of the autophagy process and then compare these two major forms of mitophagy, with particular emphasis on the molecular mechanisms of mitophagy initiation and IM dynamics. We also discuss the functional implications of these mechanistic differences in physiological and pathological context.
    Keywords:  BNIP3; Mitophagy; NIX/BNIP3L; PINK1; Parkin; Phagophore
    DOI:  https://doi.org/10.1016/j.jbior.2026.101186
  2. bioRxiv. 2026 Oct 03. pii: 2026.01.16.700014. [Epub ahead of print]
      Mitophagy is a quality control mechanism that maintains neuronal health by removing damaged mitochondria. In neurons, mitophagy can be driven by Optineurin (OPTN), a selective autophagy receptor recruited in response to oxidative stress. However, mechanistic studies of mitophagy have relied mainly on non-neuronal cell lines and acute damage paradigms. It remains unknown whether these findings translate to neurons under physiological stress conditions. Here, we investigated the temporal dynamics of OPTN-dependent mitophagy under mild oxidative stress using live-cell imaging in primary rat hippocampal neurons. We found that autophagosomes failed to readily engulf OPTN-positive (OPTN+) mitochondria, revealing a previously unidentified rate-limiting step in neuronal OPTN-mediated mitophagy. Additionally, OPTN+ mitochondria colocalized with acidified lysosomes over timescales significantly longer than previously reported. These OPTN+ mitochondria displayed locally elevated reactive oxygen species (ROS). Scavenging mitochondrial ROS increased lysosomal colocalization with damaged mitochondria and accelerated mitophagy progression. Together, these findings indicate that redox signaling contributes to the slow timescale of OPTN-mediated mitophagy in neurons.
    DOI:  https://doi.org/10.64898/2026.01.16.700014
  3. Methods Mol Biol. 2026 ;3057 189-200
      Mitophagy is the selective degradation of mitochondria via autophagy and is essential for maintaining mitochondrial quality and cellular homeostasis as well as being required for skeletal muscle differentiation and myogenesis. While traditional techniques such as immunoblotting, electron microscopy, and live-cell imaging provide valuable insights, they often offer only static or indirect measurements of mitophagy. Mitophagy flux assays capture dynamic turnover events and are, therefore, more informative. In this chapter, we present a streamlined method for monitoring and measuring mitophagic flux in C2C12 myoblasts during differentiation. Further, this approach allows for simultaneous quantification of mitochondrial morphology, providing a powerful platform for studying mitochondrial quality control in vitro.
    Keywords:  Adenovirus; Fluorescence mitophagy reporter; Mitochondrial network analysis; Mitochondrial quality control; Mitochondrial remodeling; Mitophagic flux; Mitophagy; Myogenesis
    DOI:  https://doi.org/10.1007/978-1-0716-5396-8_15
  4. FEBS J. 2026 Oct 13.
      Ageing is characterized by the progressive accumulation of molecular and cellular damage, driven by both genetic and nongenetic factors and ultimately leading to functional decline and an increased risk of disease. Convergent evidence indicates that many of the mechanisms influencing ageing are intimately related to the ability of the organism to cope with intrinsic and extrinsic stress. Key determinants of this capacity are the molecular pathways that coordinate stress responses throughout life. Among these, general and cargo-specific autophagy have emerged as integral components of cellular and systemic adaptation to stress. Here, we focus on mitophagy, a selective form of autophagy targeting mitochondria, and nucleophagy, the selective autophagic recycling of nuclear material. These processes help safeguard the integrity of two organelles that are central to long-term cellular survival and function. Such homeostatic mechanisms are vital in long-lived neurons, where they mediate damage removal during ageing to protect against neurodegeneration. We further discuss how perturbations in these autophagic pathways may contribute to ageing and neurodegenerative disorders. Finally, we outline key open questions and future challenges in the field, including the largely unexplored possibility of functional connections between mitophagy and nucleophagy, which we identify as an important direction for future research.
    Keywords:  ageing; autophagic pathways; homeostasis; mitophagy; neurodegeneration; nucleophagy; organelle quality control
    DOI:  https://doi.org/10.1111/febs.70738
  5. Front Mol Biosci. 2026 ;13 1922188
      Telomeres are repetitive DNA sequences that cap chromosome ends and protect genomic stability. The term "telomeric autophagy" has been applied to the relationship between telomere dysfunction and autophagy, but it has been used to describe two processes that are not equivalent, and much of the confusion in this literature follows from conflating them. The first is the induction of autophagy by dysfunctional telomeres. This is established: during replicative crisis, telomeric damage generates cytosolic chromatin fragments that activate cGAS-STING signalling and engage the autophagy machinery, an induction specific to telomeric damage and not produced by intrachromosomal breaks, and one that has been independently reproduced in cells maintaining telomeres through alternative lengthening. The second is the selective autophagic degradation of telomeric chromatin itself. For this we were unable to identify direct evidence: no receptor bridging telomeric chromatin to ATG8-family proteins has been described, telomeric cargo has not been recovered from autolysosomes, and no compound acts selectively on the process. This review therefore separates the two throughout, grades the evidence for each claim it makes, and applies the same grading to the disease literature, where cancer emerges as the only setting in which telomeric and autophagic endpoints have been measured in the same system. Its aim is to establish what is known with confidence, what rests on inference, and what would have to be shown for telomere-selective autophagy to be regarded as a pathway. Telomeric autophagy; telomere; aging; cellular senescence; autophagy; cancer; neurodegenerative diseases.
    Keywords:  aging; autophagy; diseases; telomeres; telomeric autophagy
    DOI:  https://doi.org/10.3389/fmolb.2026.1922188
  6. Autophagy. 2026 Oct 13. 1-3
      The mechanisms by which pancreatic β cells sense and communicate environmental cues to mitochondria to maintain insulin secretion remain poorly understood. We identified that β cells transduce metabolic stress, such as during obesity or glucolipotoxicity, through the innate immune signaling adaptor TRAF6 to regulate mitochondrial quality control. TRAF6 was dispensable for β-cell function at baseline yet was essential for glucose-stimulated insulin secretion in mouse or human β cells following nutrient excess. TRAF6 was required for the recruitment of components of both ubiquitin- and receptor-mediated mitophagy pathways to clear dysfunctional mitochondria following metabolic stress. Interestingly, concomitant loss of the ubiquitin-mediated mitophagy effector Parkin restored glucose homeostasis and mitophagy flux in TRAF6-deficient β cells by relieving impediments in receptor-mediated mitophagy. Together, we found that TRAF6 forms a molecular relay linking environmental signals to multiple mitophagy pathways to equip β cells with the means to adapt to metabolic demand and prevent diabetes.Abbreviations: ADP: adenosine diphosphate; ATP: adenosine triphosphate; BNIP3: BCL2 interacting protein 3; GSIS: glucose-stimulated insulin secretion; HFD: high-fat diet; MFN2: mitofusin 2; PRKN: parkin RBR E3 ubiquitin protein ligase; RNF41/NRDP1: ring finger protein 41; SQSTM1/p62: sequestosome 1; T2D: type 2 diabetes; TAX1BP1: Tax1 binding protein 1; TLR: Toll-like receptor; TRAF6: TNF receptor associated factor 6.
    Keywords:  Autophagy; beta cell; innate immunity; mitochondria; parkin; traf6
    DOI:  https://doi.org/10.1080/15548627.2026.2747028
  7. Cells. 2026 Sep 30. pii: 1781. [Epub ahead of print]15(19):
       BACKGROUND: Mitochondria-lysosome coupling and mitophagy are fundamental to mitochondrial homeostasis, yet the determinants governing this process remain incompletely defined. This study distinguished the regulatory modes of TBC1D15 and established its functional role as a downstream effector in mitochondria-linked autophagy.
    METHODS: PC-12 and HeLa cells were treated with CCCP, gradient-concentrated AuNPs, and CQ, combined with siRNA-mediated PINK1 knockdown. Whole-cell, mitochondrial and lysosomal fractions were analyzed by immunoblotting.
    RESULTS: Inter-organelle translocation of TBC1D15, rather than its total abundance, serves as the critical switch for mitochondria-lysosome homeostasis. CCCP induced a time-dependent biphasic change in TBC1D15 that persisted upon PINK1 knockdown, indicating regulation is not strictly PINK1-dependent. High-dose AuNPs trapped TBC1D15 on mitochondria and blocked lysosomal delivery via a PINK1-independent route. AuNPs exhibited biphasic concentration-dependent effects: low concentrations moderately upregulated TBC1D15, promoting adaptive organelle contacts, while millimolar concentrations caused pathological tethering. Subcellular fractionation and CQ intervention confirmed that defective lysosomal delivery underlies mitochondrial TBC1D15 accumulation upon AuNP challenge.
    CONCLUSIONS: This work establishes two distinct regulatory axes converging on TBC1D15. High-dose AuNPs can serve as a specific pharmacological blocker of TBC1D15 trafficking, offering therapeutic avenues for disorders characterized by impaired mitophagy.
    Keywords:  TBC1D15; lysosomes; mitochondria; mitochondrial homeostasis
    DOI:  https://doi.org/10.3390/cells15191781
  8. Aging Dis. 2026 09 28.
      Age-related deterioration of skeletal muscle contributes to loss of mobility, frailty, and disability. Altered autophagy-lysosome competence has been proposed as a mechanism linking impaired proteostasis, mitochondrial damage, inflammation, and regenerative failure to sarcopenia. Chronological muscle aging and clinically defined sarcopenia overlap, but evidence from healthy aging, frailty, disuse, cachexia, obesity, or chronic disease cannot be treated as interchangeable. This narrative review examines how lysosomal acidification, degradative capacity, biogenesis, and turnover influences autophagic flux in aging muscle and evaluates the strength of evidence across experimental models and human studies. Genetic and pharmacological studies show that severe disruption of autophagy or specific lysosomal functions can cause myofiber damage, mitochondrial impairment, defective regeneration, and weakness. However, direct evidence that lysosomal acidification, fusion, hydrolase activity, membrane integrity, recycling, cargo degradation, or completed autophagic flux is impaired in aging human muscle remains limited. Much of the human literature relies on static abundance of LC3-II, SQSTM1/p62, lysosomal proteins, or transcriptional signatures, which cannot distinguish increased autophagosome formation from impaired degradation. We therefore separate causal experimental evidence from human associations and focus on V-ATPase, TMEM175, LAMP proteins, TFEB/TFE3, lysophagy, and crosstalk with mitophagy and the ubiquitin-proteasome system. Exercise improves clinically relevant outcomes in older adults, but mediation through completed autophagic flux has not been established. Recent trials of metformin and once-weekly sirolimus did not improve prespecified functional outcomes in the tested populations and regimens, whereas urolithin A produced endpoint-specific signals while missing key primary outcomes.
    DOI:  https://doi.org/10.14336/AD.2026.1047
  9. Biochem Soc Trans. 2026 Oct 28. 54(10): 1497-1511
      Autophagy is the cell's recycling system; it removes unwanted or dysfunctional cellular material, thereby preventing damage. Importantly, it is a key pro-survival pathway during periods of stress, for instance, during nutrient scarcity. As it can support nutrition during starvation, it is not surprising that autophagy is controlled by nutrient availability. As a result, diet-based strategies to modify autophagy have attracted considerable scientific and public interest, although what is presented to the public is often not supported by a solid scientific foundation. Evidence from animal models is compelling: several of these interventions robustly activate autophagy and are linked to improved lifespan and healthspan. Data from humans, however, are much more limited. Many human studies rely on measurement of steady-state levels of autophagy genes or proteins, metrics that do not independently establish pathway activity. Far fewer have measured autophagic 'flux', the more rigorous readout of turnover, and where they have, findings are often negative or inconclusive. Here, we review the human research on popular nutritional interventions purported to change autophagy-including prolonged fasting, intermittent fasting, calorie restriction, and altered macronutrient intake-and contrast these findings with the preclinical evidence that has shaped public expectations. We highlight key gaps in the literature, particularly the scarcity of flux-based measurements and the reliance on blood as a proxy for autophagy in other, less accessible tissues. Refining how we monitor autophagy in humans should be a key priority for the field and is ultimately needed to establish whether and how diet modulates human autophagy.
    Keywords:  autophagy; calorie restriction; fasting; intermittent fasting
    DOI:  https://doi.org/10.1042/BST20260632
  10. Pharmacol Rev. 2026 Aug 22. pii: S0031-6997(26)00046-3. [Epub ahead of print]78(6): 100158
      Autophagy is a fundamental cellular process that maintains homeostasis by degrading and recycling cellular components. As autophagy is essential for metabolizing damaged organelles and toxic substances, it plays a crucial role in both normal physiology and pathological conditions. However, autophagy has dual roles in both tumorigenesis and neurodegeneration. In cancer, autophagy can act as a tumor suppressor by clearing damaged components in early stages, but promotes tumor survival and growth in later stages, particularly under stress. In neurodegeneration, impaired autophagy is implicated in the disease progression of conditions such as Alzheimer, Parkinson, and Huntington diseases, in which the failure to clear misfolded proteins and damaged organelles exacerbates disease pathology. This review is organized to cover the molecular machinery and transcriptional regulation of autophagy, its disease-specific subtypes, its dual roles in tumorigenesis and neurodegeneration, and the current pharmacological landscape for therapeutic targeting. Attention is given to pharmacological modulation of autophagy, including senolytic drugs that selectively eliminate senescent cells by exploiting their dependence on antiapoptotic survival pathways, and small-molecule regulators targeting key pathways such as phosphoinositide 3-kinase/Akt serine/threonine kinase/mechanistic target of rapamycin and AMP-activated protein kinase. Depending on the pathological context, these drugs are under development to either inhibit or induce autophagy. Additionally, we address the challenges and limitations in developing effective autophagy-targeting drugs, underscoring the need for further research to identify new compounds that can modulate cellular autophagic flux. SIGNIFICANCE STATEMENT: Autophagy is an important homeostatic mechanism, and its dysregulation contributes to a wide range of diseases, including cancer and neurodegenerative disorders. Therefore, a deeper mechanistic understanding of the regulation of autophagy is crucial for advancing targeted therapies with significant clinical impact.
    DOI:  https://doi.org/10.1016/j.pharmr.2026.100158
  11. Front Endocrinol (Lausanne). 2026 ;17 1957312
      Diabetic kidney disease (DKD) is conventionally framed as a glomerular microvascular complication but may also involve tubular degradative maladaptation, in which tubular cells progressively fail to clear damaged organelles, lipid droplets, and stress-related cargo through the autophagy-lysosome system. Among tubular compartments, proximal tubular epithelial cells depend particularly heavily on mitochondrial metabolism, endocytic trafficking, vesicular transport, and lysosome-supported proteostasis, making them especially vulnerable to diabetic metabolic stress. This review examines whether autophagy-lysosome failure, encompassing both initiation-level and flux-completion defects, provides a candidate link between adaptive tubular stress responses and maladaptive tubular cell-state remodeling. We appraise therapeutic opportunities for restoring degradative capacity, including standard metabolic and hemodynamic therapies, transcription factor EB (TFEB)- and AMP-activated protein kinase (AMPK)-centered interventions, selective autophagy modulation, and mechanism-guided integrative strategies. We propose a testable, stage-dependent reversibility framework, rather than an established DKD staging system: restoration of autophagy-lysosome flux and lysosomal capacity may be most effective before persistent senescence, ferroptotic vulnerability, and fibrosis become difficult to reverse. Accordingly, we distinguish initiation defects from completion defects using flux-competent criteria and identify the stage-dependent reversibility window as the principal conceptual contribution of this review, rather than a validated clinical staging construct.
    Keywords:  ER-phagy; TFEB; autophagic flux; autophagy-lysosome axis; diabetic kidney disease; lipophagy; mitophagy; renal tubule epithelial cells
    DOI:  https://doi.org/10.3389/fendo.2026.1957312
  12. Autophagy Rep. 2026 ;5(1): 2740425
      The intracellular Ca2+ channel TRPML3 regulates autophagy by multimerization in a phosphoinositide (PIP)-dependent manner; however, its role in other membrane dynamics remains unclear. Here, we report that TRPML3 regulates type III unconventional protein secretion (UcPS) through two distinct pathways: TMED10-channeled UcPS and secretory autophagy. TRPML3 interacted with TMED10 and macrophage migration inhibitory factor (MIF), a signal sequence-lacking pleiotropic cytokine whose secretion mechanism has remained undefined. We found that cytosolic MIF is transported to membrane-enclosed compartments through TMED10-channeled UcPS. Notably, TRPML3, but not TRPML1 or TRPML1/3, promoted TMED10 oligomerization, thereby enhancing MIF secretion in a Ca2+-independent manner. Furthermore, once translocated into vesicular compartments, MIF colocalized with LC3, and its secretion was dependent on secretory autophagy. Mechanistically, we identified PI(3,4)P2 as a key regulator of secretory autophagy, with TRPML1/3 acting downstream of PI(3,4)P2 to mediate Ca2+-dependent MIF secretion. Taken together, our findings demonstrate that MIF is a novel cargo of type III UcPS, operating through TMED10-channeled UcPS and secretory autophagy, which are regulated by TRPML3 in a Ca2+-independent manner and by the PI(3,4)P2-TRPML1/3 axis in a Ca2+-dependent manner, respectively.
    Keywords:  MIF; PI(3,4)P2; TMED10-channeled unconventional protein secretion; TRPML1/3; TRPML3; secretory autophagy
    DOI:  https://doi.org/10.1080/27694127.2026.2740425
  13. Front Cell Dev Biol. 2026 ;14 1935788
      Mitochondrial dysfunction is a hallmark of Parkinson's disease (PD), but how impaired mitochondrial homeostasis drives the selective death of dopaminergic neurons is still poorly understood. At the center of this problem lies the mitochondrial protein import machinery-the TOM and TIM23 translocases-which doubles as a stress-sensing hub that coordinates two distinct quality control pathways. When import is compromised, the kinase PINK1 accumulates on the mitochondrial surface, recruits Parkin to ubiquitinate outer membrane proteins, and triggers mitophagy. Meanwhile, the stress sensor DELE1 is cleaved and released to the cytosol, where it activates the HRI kinase to phosphorylate eIF2α and engage the integrated stress response (ISR). These two pathways are not independent. Recent work shows they engage in antagonistic crosstalk: the DELE1-HRI-ISR axis suppresses PINK1/Parkin-dependent mitophagy by preserving mitochondrial import efficiency, acting as a molecular brake on organelle clearance. The balance between these pathways is governed by the SIFI E3 ubiquitin ligase complex, which targets both DELE1 and HRI for degradation. Disruption of SIFI causes progressive neurodegeneration in humans. Here we synthesize the structural, biochemical, and genetic evidence that defines the TOM/TIM-PINK1/Parkin-DELE1/HRI signaling axis, examine how its dysregulation contributes to dopaminergic neuron vulnerability, and evaluate therapeutic strategies targeting mitochondrial import stress in PD.
    Keywords:  DELE1; HRI; PINK1; Parkinson’s disease; integrated stress response; mitochondrial protein import; mitophagy; parkin
    DOI:  https://doi.org/10.3389/fcell.2026.1935788
  14. Redox Biol. 2026 Sep 29. pii: S2213-2317(26)00419-2. [Epub ahead of print]97 104420
      Ferroptosis resistance contributes to pathological skin scarring, but the underlying regulatory mechanisms remain unclear. Here, we identified a novel selective autophagy pathway NEURL1-SQSTM1/p62-SLC40A1 that controls fibroblast ferroptosis and scar formation. SLC40A1 is upregulated in human scars, conferring ferroptosis resistance by promoting iron efflux. Mechanistically, NEURL1 mediates K63-linked ubiquitination of SLC40A1, enabling its recognition by SQSTM1 for lysosomal degradation. A microneedle system co-delivering curcumin (autophagy activator) and siSLC40A1 effectively activates this axis, induces ferroptosis, and alleviates scarring in vivo. Our findings reveal a new therapeutic target and strategy for pathological scars.
    Keywords:  Autophagy; Ferroptosis; Microneedles; Pathological scars; SLC40A1
    DOI:  https://doi.org/10.1016/j.redox.2026.104420
  15. Mol Microbiol. 2026 Oct 11.
      The mechanistic target of rapamycin (mTOR) signaling pathway is a central regulator of nutrient sensing, metabolism, growth, and stress adaptation in most eukaryotes. Malaria parasites of the genus Plasmodium, however, lack identifiable orthologues of mTOR kinase and its associated signaling complexes, raising the question of how these organisms coordinate environmental sensing with developmental progression and proliferation. Here, we discuss emerging evidence suggesting that Plasmodium has evolutionarily replaced the canonical mTOR signaling axis with a distributed regulatory architecture composed of parasite-specific nutrient sensors, kinase-based signaling pathways, translational repression mechanisms, and unconventional autophagy processes. Components such as KIN, PI3K, eIF2α kinases, eIF4E-interacting protein DOZI, and Maf1 collectively preserve many hallmark outputs of mTOR signaling, including metabolic adaptation, stress tolerance, developmental plasticity, and reversible quiescence. In addition, malaria parasites interact with host mTOR pathways during infection, potentially exploiting host-derived anabolic signaling environments to support intracellular development. These findings suggest that Plasmodium exemplifies an extreme case of signaling plasticity in eukaryotic evolution, demonstrating how essential mTOR-associated functions can be maintained despite the apparent loss of the pathway itself.
    Keywords:   Plasmodium ; kinase network; malaria; mechanistic target of rapamycin; nutrient sensing; stress adaptation
    DOI:  https://doi.org/10.1111/mmi.70123
  16. Proc Natl Acad Sci U S A. 2026 Oct 20. 123(42): e2621286123
      S-adenosyl-L-methionine (SAM) is a fundamental methyl donor; however, the physiological role of its byproduct and competitive inhibitor, S-adenosyl-L-homocysteine (SAH), remains unclear. Here, we show that transient reactive oxygen species (ROS) production triggered by SAH during the early logarithmic phase mimics partial SAH hydrolase inhibition, extending the yeast chronological lifespan (CLS) through a hormetic mechanism. This study reveals that the dual nature of ROS in aging is determined by the specific degree of SAH hydrolase activity. We identified the adenosine 5'-triphosphate-binding cassette (ABC) transporter Ybt1 as a key downstream effector of SAH. Ybt1 localizes to the vacuolar membrane and facilitates the sequestration of SAM from the cytosol into the vacuole. Notably, YBT1 overexpression extends CLS, mimicking SAH effects through an integrated pathway involving target of rapamycin complex 1 downregulation, autophagy, and adenosine 5'-monophosphate-activated protein kinase activation. Our findings establish that SAH acts as a metabolic signal coupling nutrient and energy availability to longevity via Ybt1, defining an adaptive/hormetic response for lifespan regulation in yeast.
    Keywords:  ABC transporter; S-adenosyl-L-homocysteine; TORC1; chronological lifespan; mitochondria
    DOI:  https://doi.org/10.1073/pnas.2621286123
  17. Trends Mol Med. 2026 Oct 14. pii: S1471-4914(26)00231-5. [Epub ahead of print]
      α-Synuclein (α-Syn) accumulation is a defining feature of Parkinson's disease (PD). Zhang et al. identify cholesterol 25-hydroxylase (CH25H) as an astrocytic inhibitor of p62-dependent α-Syn degradation. Disrupting the CH25H-p62 interaction facilitates α-Syn clearance via autophagy and improves PD-like phenotypes, suggesting a previously unrecognized nonenzymatic function for CH25H with therapeutic potential.
    Keywords:  astrocytes; autophagy; cholesterol 25-hydroxylase; p62; synucleinopathy
    DOI:  https://doi.org/10.1016/j.molmed.2026.09.015
  18. Autophagy. 2026 Oct 11.
      Although the Golgi apparatus undergoes extensive disassembly during mitosis to ensure its equitable partitioning into two daughter cells, the extreme asymmetry of oocyte meiosis obviates this need, raising fundamental questions about the existence and necessity of Golgi disassembly in oocytes. Herein, we demonstrated the existence of a Golgi disassembly process during oocyte meiosis I, which peaked at germinal vesicle breakdown (GVBD) and was largely completed by metaphase II (MII). Strikingly, the vesiculation stage of Golgi disassembly exhibited a function divergent from mitosis by governing spindle cortical migration during metaphase I (MI), thereby ensuring oocyte polarity establishment. Moreover, we found that macroautophagy/autophagy negatively regulated the vesiculation stage of Golgi disassembly: its hyperactivation suppressed vesiculation, whereas its inhibition conversely accelerated this process. Mechanistically, MIA2 and SFT2D2 were identified as key downstream effectors through which autophagy controlled Golgi vesiculation. MIA2 mediated autophagy-dependent regulation of Golgi dynamics through its two LIR motifs, thereby linking autophagic signaling to Golgi remodeling. Specifically, autophagy activation downregulated MIA2, thus inhibiting the ubiquitin-dependent degradation of SFT2D2, consequently suppressing Golgi vesiculation and spindle migration during oocyte meiosis I; conversely, autophagy inhibition accelerated these processes by increasing MIA2 to promote SFT2D2 degradation. These findings elucidate the key role of autophagy in regulating Golgi disassembly, thereby providing a new organelle-based perspective on how autophagy contributes to oocyte spindle migration. Furthermore, our work identifies a novel Golgi-dependent mechanism for oocyte polarity establishment and uncovers the divergent functions of Golgi remodeling across distinct division modes.
    Keywords:  Autophagy; MIA2; SFT2D2; golgi disassembly; meiosis; oocyte; spindle migration
    DOI:  https://doi.org/10.1080/15548627.2026.2747860
  19. Exp Cell Res. 2026 Oct 13. pii: S0014-4827(26)00312-5. [Epub ahead of print] 115195
      The development of craniofacial bones is highly dependent on the intramembranous ossification process driven by orofacial mesenchymal stem cells (OMSCs). Optineurin (OPTN), a traditional mitophagy receptor, promotes OMSC matrix mineralization by mediating the extracellular release of amorphous calcium phosphate (ACP) through the initiation of mitophagy via liquid-liquid phase separation. However, the dynamic mechanisms by which OPTN regulates mitochondrial engulfment remain elusive. In this work, we show that in both zebrafish and mouse models, Optn absence causes systemic bone loss and craniofacial abnormalities. Mechanistically, OPTN recruits thyroid receptor-interacting protein 6 (TRIP6) to the surface of damaged mitochondria, inducing local F-actin polymerization and remodeling, which relies on cytoskeletal mechanical forces to support the bending and closure of the phagophore. The depletion of OPTN or TRIP6 significantly impairs mitophagy flux, triggering a massive accumulation of dysfunctional mitochondria. Overall, this study elucidates that the OPTN-TRIP6-F-actin axis ensures autophagosome closure through cytoskeletal remodeling, revealing a novel paradigm in which cytoskeletal mechanical regulation maintains mitochondrial homeostasis to orchestrate craniofacial osteogenesis.
    Keywords:  Craniofacial bone development; Mitophagy; OPTN; TRIP6
    DOI:  https://doi.org/10.1016/j.yexcr.2026.115195
  20. bioRxiv. 2026 Sep 29. pii: 2026.09.28.755133. [Epub ahead of print]
      Ether glycerophospholipids (ether lipids) are a subclass of glycerophospholipids that are synthesized at the peroxisome and constitute nearly 20% of the total phospholipid content in metazoans. Biochemically, ether lipids have an alkyl chain attached by an ether bond at the sn-1 position of the glycerol backbone (alkyl-ether) primarily containing choline or ethanolamine head groups. Some ether lipids contain a cis bond adjacent to the ether linkage (alkenyl-ether) and are commonly referred to as plasmalogens. While the importance of ether lipids in humans is clear, highlighted by the severity of inherited peroxisomal disorders caused by ether lipid deficiency, the molecular roles of these lipids remain poorly understood. Here, we identify a link between ether lipid metabolism, peroxisome degradation, and oxygen availability. We find Fatty acyl-CoA-reductase 1 (FAR1), the rate-limiting enzyme in peroxisomal ether lipid metabolism, acts as a peroxisome receptor necessary for peroxisome degradation when oxygen is limiting. Hypoxia increases choline ether lipid abundance, promotes autophagy activation, and peroxisome degradation. Mechanistically, FAR1 binds ATG8-family protein LC3B and is necessary and sufficient to control peroxisome degradation under hypoxia. FAR1's enzymatic function as well as its capacity to bind LC3B is necessary to degrade peroxisomes under hypoxia. Similarly, loss of multiple components of peroxisomal ether lipid metabolism blocks peroxisome degradation under hypoxia in cells and in vivo. In mouse models of chronic HIF activation, Far1 is a direct HIF target gene and is necessary for peroxisome degradation in this setting. Increasing ether lipids using ether lipid precursors activates autophagy and promotes autophagy-dependent cardioprotection against ischemic injury. This work reveals FAR1 as a critical regulator of peroxisome homeostasis in the setting of oxygen limitation.
    DOI:  https://doi.org/10.64898/2026.09.28.755133
  21. Front Aging Neurosci. 2026 ;18 1915475
      Parkinson's disease (PD) is a debilitating neurodegenerative disorder with no available cure, underscoring the urgent need for novel therapeutics. This study employed the comprehensive bioinformatic analyses and the experimental models to investigate the potential of clemastine (CLE) for PD treatment. Bioinformatics identified 12 distinct cell subtypes and 577 differentially expressed genes in dopaminergic neurons (DaNs), along with 167 potential PD-relevant CLE targets. A significant correlation was found between Braak stage and autophagy-related gene expression in the substantia nigra. In MPP+-induced PC12 cell model, CLE treatment increased AMPK phosphorylation and decreased mTOR phosphorylation at Ser2448, suggesting the activation of AMPK and reduced mTOR activity, which was accompanied by the reduced levels of α-synuclein (α-syn) and p62, increased lysosomal (LAMP1) and autophagosomal (LC3) markers, and enhanced cell viability. CLE increased the LC3-II/LC3-I ratio even in the presence of bafilomycin A1, indicating enhanced autophagosome synthesis. Conversely, the AMPK inhibitor dorsomorphin blocked CLE effects, restoring mTOR phosphorylation and α-syn levels. In the chronic MPTP-induced mouse model, CLE administration increased the phosphorylation of AMPK, increased the LC3-II/LC3-I ratio, and decreased mTOR phosphorylation, p62, and α-syn levels. Immunofluorescence revealed the increased DaNs (tyrosine hydroxylase-positive) and LC3 puncta, alongside reduced the phosphorylated α-syn (p-S129). These cellular and molecular improvements correlated with the alleviation of both motor (rotarod test) and non-motor (fecal pellet output) deficits. Collectively, our findings suggest that CLE alleviates PD pathology by increasing AMPK phosphorylation and decreasing mTOR phosphorylation at Ser2448, suggesting the activation of AMPK pathway and reduced mTOR activity, thereby enhancing the autophagic flux by promoting both the synthesis and degradation of autophagosomes. Subsequently it facilitates the clearance of pathological α-syn, improves the neuronal survival, and ameliorates the behavioral symptoms. We propose CLE as a promising therapeutic candidate for PD via autophagy modulation.
    Keywords:  AMPK/mTOR pathway; Parkinson’s disease; autophagy; bioinformatics; clemastine; drug repurposing; neuroprotection; α-Synuclein
    DOI:  https://doi.org/10.3389/fnagi.2026.1915475
  22. Sci Adv. 2026 Oct 16. 12(42): eaef8820
      Mitophagy, the selective degradation of mitochondria by lysosomes, is a major mitochondrial quality-control pathway, yet its role in lung cancer initiation and therapeutic response remains poorly understood. We investigated PINK1-dependent mitophagy in human lung adenocarcinoma and directly monitored mitophagy in vivo using mito-QC reporter mice during lung tumor development. We found that PINK1 activity and mitophagy are increased in human tumors and are activated from the earliest stages of tumorigenesis. Genetic inhibition of PINK1 impaired oncogenic transformation but had little impact once tumor cells were established, identifying mitophagy as a critical early adaptation during lung cancer initiation. PINK1 deficiency markedly enhanced the efficacy of KRAS-targeted therapy in vitro and in vivo. Together, our findings identify PINK1-dependent mitophagy as an early vulnerability in KRAS-driven lung cancer and provide a rationale for targeting mitophagy to improve the efficacy of KRAS-targeted therapies.
    DOI:  https://doi.org/10.1126/sciadv.aef8820
  23. Int J Mol Sci. 2026 Sep 26. pii: 8621. [Epub ahead of print]27(19):
      Autophagy is a conserved lysosome-dependent process essential for cellular homeostasis, and pharmacological activation of autophagy has emerged as a promising therapeutic strategy for age-related, neurodegenerative, metabolic, and malignant diseases. Despite the growing interest in natural autophagy modulators, lichens remain largely unexplored as a source of autophagy-inducing compounds. Here, we tested ethanolic extracts from four commercially available lichens using LC3-II accumulation as a primary readout. Usnea sp. was identified as the most active species. Activity-guided fractionation followed by HRMS and NMR analyses identified salazinic acid as the active metabolite. Salazinic acid increased LC3-II accumulation, enhanced autophagic flux in the presence of bafilomycin A1, and promoted autophagosome formation as confirmed by transmission electron microscopy. The compound exhibited low cytotoxicity in human cell lines at concentrations exceeding those required for autophagy induction. Mechanistically, salazinic acid activated the phosphorylation of AMPK, ULK1, and AKT; however, it retained its ability to stimulate autophagic flux in AMPK- and ULK1-deficient cells, indicating that its activity is not strictly dependent on the canonical AMPK-ULK1 signaling pathway. Collectively, our findings identify salazinic acid as a previously unrecognized inducer of productive autophagic flux and demonstrate that lichen secondary metabolites represent a promising and largely untapped source of novel autophagy-modulating compounds.
    Keywords:  Usnea sp.; lichen extracts; lichens; novel resource of autophagy inducers; salazinic acid
    DOI:  https://doi.org/10.3390/ijms27198621
  24. J Biol Chem. 2026 Oct 14. pii: S0021-9258(26)02518-4. [Epub ahead of print] 113646
      Intracellular iron is distributed across functionally distinct pools though the mechanisms regulating its compartmentalization remain unclear. Here we show that EPG5, a tethering factor required for autophagosome-lysosome fusion, governs iron compartmentalization through dual mechanisms: direct involvement in autophagy and indirect regulation of ferritinophagy initiation. A systematic comparison of autophagy genes indicates that EPG5 deficiency uniquely decreases hemosiderin and increases the labile iron pool, a profile distinct from ATG5, ATG14, FIP200, or WDR45 deficiencies. Mechanistically, EPG5 loss disrupts autophagosome maturation and endocytic trafficking, causing ferritin condensates and iron transporters to accumulate in aberrant autophagosomes and endosomes. This blockade triggers compensatory TBK1 activation. TBK1 subsequently phosphorylates TAX1BP1 and interacts with the ferritinophagy receptors NCOA4, inhibiting receptor homo-oligomerization and modulating ferritinophagic flux. These findings position EPG5 as a novel orchestrator of iron compartmentalization and highlight the role of TBK1-NCOA4/TAX1BP1 axis in iron homeostasis and related stress response.
    Keywords:  EPG5; NCOA4; TBK1; ferritinophagy; iron compartmentalization
    DOI:  https://doi.org/10.1016/j.jbc.2026.113646
  25. Aging Cell. 2026 Oct;25(10): e70755
      Lysosomal decline and proteostasis collapse are defining features of aging and major contributors to neurodegenerative vulnerability, yet interventions that preserve neuronal lysosomal function across aging remain poorly defined. Here, we identify 20(S)-ginsenoside Rg3, a ginseng-derived natural product, as a geroprotective small molecule in Caenorhabditis elegans. Rg3 extended lifespan and preserved key physiological outputs, including locomotion and pharyngeal pumping, indicating that Rg3 delays functional aging. Rg3 also maintained mechanosensory neuron integrity and touch sensitivity, suppressed neuronal polyglutamine aggregation, and protected dopaminergic neurons against α-synuclein-induced degeneration. At the cellular level, Rg3 restored age-impaired lysosomal function and autophagic flux in neurons. Mechanistically, Rg3 shifted neuronal phosphoinositide reporter signatures toward a PI(4)P-enriched and PI(3)P-reduced state, consistent with signaling lipid remodeling at lysosomal membranes. This phosphoinositide shift coincided with reduced RSKS-1/S6K phosphorylation, indicating suppression of TOR complex 1 (TORC1), and promoted nuclear localization of HLH-30, the C. elegans ortholog of transcription factor EB (TFEB), thereby engaging a conserved lysosomal program. Collectively, these results define Rg3 as a natural-product geroprotector that couples lysosomal lipid remodeling to TORC1-HLH-30 signaling to preserve lysosomal competence, neuronal proteostasis, and organismal fitness during aging. Our study nominates phosphoinositide control of lysosomal identity as a therapeutic entry point for healthy aging and neuroprotection.
    Keywords:   Caenorhabditis elegans ; TFEB; TORC1; autophagy; ginsenoside Rg3; healthy aging; lysosome; phosphoinositides
    DOI:  https://doi.org/10.1111/acel.70755
  26. Int J Mol Sci. 2026 Oct 07. pii: 8892. [Epub ahead of print]27(19):
      Unc-51-like autophagy-activating kinase 1 (ULK1), a serine/threonine kinase, is the central regulator of autophagy initiation and plays a crucial role in cellular homeostasis, metabolic adaptation, and stress responses. We performed a large-scale phosphoproteomic data analysis of ULK1 by systematically integrating and analyzing 891 profiling and 245 differential human phosphoproteomic datasets. S450, S623, and S638 emerged as the predominant phosphosites in ULK1, with the highest frequency of detection across multiple cellular phosphoproteomics datasets. Conservation analysis showed that these phosphosites are conserved across mammalian species and human ULK1 and ULK2 (Unc-51-like autophagy-activating kinase 2). The co-regulatory networks associated with these phosphosites, including interacting proteins, upstream kinases, and downstream substrates, were systematically analyzed. The phosphosite co-regulated ULK1 interactome revealed a network of associations linking ubiquitin-dependent cargo recognition to autophagosome biogenesis, trafficking, and maturation, indicating that ULK1 phosphoregulation may extend beyond its established role in autophagy initiation and be associated with multiple stages of selective autophagy. Notably, ULK1 phosphosites were linked to key metabolic enzymes in glycogen, sphingolipid, phospholipid, and glycolytic pathways, as well as classical lipolysis. Protein-normalized analysis across 12 cancer cohorts showed significant upregulation of the predominant ULK1 phosphosites, most frequently at S450 and S623. Comparative analysis with an independent ULK1/2 knockout phosphoproteomic dataset further supported the relevance of these identified co-regulated protein phosphosites. Collectively, this study provides a phosphosite-resolved view of ULK1 regulation and identifies candidate phosphosites and associated proteins for future functional and mechanistic studies.
    Keywords:  ULK1; autophagy; lipolysis; metabolic enzymes; phospho-regulatory network
    DOI:  https://doi.org/10.3390/ijms27198892
  27. Front Neurol. 2026 ;17 1943801
      Parkinson's disease (PD) is the second most prevalent neurodegenerative disorder worldwide, characterized by the progressive loss of dopaminergic neurons in the substantia nigra, accumulation of α-synuclein (α-syn), mitochondrial dysfunction, and neuroinflammation. Nicotinamide adenine dinucleotide (NAD+), a crucial coenzyme involved in cellular energy metabolism, DNA repair, and epigenetic regulation, declines with aging and is markedly reduced in the brains of patients with PD. Emerging evidence suggests that supplementation with NAD+ precursors, including nicotinamide riboside (NR) and nicotinamide mononucleotide (NMN), exerts neuroprotective effects through multiple mechanisms, such as activation of the mitochondrial unfolded protein response (UPR∧mt), enhancement of autophagy, and suppression of excessive poly(ADP-ribose) polymerase 1 (PARP1) activation. This review summarizes the central role of NAD+ dysregulation in the pathogenesis of PD, with particular emphasis on the interplay between NAD+ depletion, mitochondrial quality control, proteostasis, and neuroinflammation. Furthermore, we discuss recent advances in NAD+-boosting strategies in PD models and clinical studies, highlighting their potential therapeutic implications for PD intervention.
    Keywords:  NAD+; Parkinson's disease; mitochondrial quality control; neuroprotection; nicotinamide riboside
    DOI:  https://doi.org/10.3389/fneur.2026.1943801
  28. bioRxiv. 2026 Sep 30. pii: 2026.09.29.755113. [Epub ahead of print]
      Peroxisomes, along with mitochondria, coordinate and compartmentalize oxidative metabolism in eukaryotic cells. Rare genetic disorders caused by mutations in PEX genes impair peroxisome function and cause Peroxisome Biogenesis Disorders, which are characterized by liver and neurological dysfunction, hearing and vision loss, and metabolic abnormalities. The majority of Peroxisome Biogenesis Disorders (PBDs) are caused by mutations in the gene encoding PEX1, which together with PEX6 forms a hetero-hexameric AAA-ATPase complex that drives the import of enzymes into the peroxisome lumen. One particular destabilizing mutation - PEX1G843D - results in almost 30% of all cases. Here we show that deficiencies in PEX1 lead to increased levels of the oxygen-responsive transcription factor HIF1α in normoxia, as well as a HIF1α transcriptional signature. The increase in HIF1α protein was rescued by overexpression of PEX1WT, suggesting PEX1 deficiencies modulate HIF1α signaling. The increased levels of HIF1α were not explained by defects in the oxygen responsive degradation pathway of HIF1α that relies on proline hydroxylase domain enzyme-dependent hydroxylation and von Hippel Lindau tumor suppressor protein-dependent ubiquitination. Instead, we found that PEX1 deficiency alters HIF1α proteostasis by reducing degradation through a hydroxylation- and autophagy- dependent mechanism. Notably, enhancing autophagic capacity by ULK1 agonism was sufficient to reduce HIF1α levels in PEX1 deficient cells. Lastly, we demonstrate that upon hypoxia-reoxygenation, PEX1 deficient cells are slower to reset HIF1α levels. Our results suggest that PBD patients with PEX1 deficiency may be susceptible to dysregulation of the HIF1α pathway, particularly in tissues where oxygen gradients are physiological or developmentally required.
    Keywords:  Peroxisome; autophagy; cell signaling; hypoxia; hypoxia-inducible factor (HIF); proteostasis
    DOI:  https://doi.org/10.64898/2026.09.29.755113
  29. Glia. 2026 Dec;74(12): e70244
      Krabbe disease (KD) is a lysosomal storage disorder characterized by severe peripheral demyelination caused by mutations in galactosylceramidase (GALC), leading to the accumulation of galactosylceramide and psychosine. Although psychosine toxicity is central to KD pathology, additional mechanisms likely contribute to myelin dysfunction. Because Schwann cells (SCs) play a critical role in myelin maintenance, and GALC deficiency disrupts lysosomal function, we hypothesized that autophagy is altered in SCs during KD progression. Using a SC-specific Galc conditional knockout (Galc SC cKO) mouse model, we identified early changes in autophagy-related protein levels and increased autophagosome abundance during the pre-symptomatic phase, prior to detectable myelin abnormalities. To assess whether autophagy contributes to disease progression, we selectively deleted Atg7, an essential regulator of canonical autophagy, in SCs. Atg7 deletion alone did not affect myelin or behavior, but its loss in Galc SC cKO mice markedly worsened disease severity. Atg7-Galc SC cKO mice exhibited significantly thinner myelin and pronounced deficits in motor performance and nerve conduction, accompanied by altered steady-state levels of autophagy-associated proteins and functional decline. Notably, Atg7 deletion in Galc SC cKO mice did not further increase macrophage abundance, suggesting that the worsened myelin phenotype occurs without additional macrophage recruitment at this stage. Together, these findings demonstrate that autophagy-associated changes occur early in KD and ATG7-dependent pathways play a protective role during disease progression. Modulating ATG7-dependent pathways may therefore warrant further investigation as a strategy to support myelin maintenance in KD and related lysosomal disorders.
    DOI:  https://doi.org/10.1002/glia.70244
  30. bioRxiv. 2026 Sep 29. pii: 2026.09.28.755091. [Epub ahead of print]
      Peroxisome proliferator-activated receptor gamma (PPARγ) is a central regulator of lipid metabolism and a critical mediator of neuroprotection, yet the mechanisms linking these functions remain unclear. Here, we identify the Caenorhabditis elegans nuclear receptor SEX-1 as a functional PPARγ-like regulator and define a pathway that coordinates lipid metabolism with mitochondrial homeostasis to preserve neuronal function. Integrating comparative genomics, multi-omics profiling, meta-analysis, and experimental validation, we show that SEX-1 orchestrates membrane sphingolipid metabolism, lipid droplet (LD) dynamics, and mitochondrial quality control through interconnected lipogenic and autophagic programs. Loss of sex-1 disrupts this metabolic network, resulting in aberrant LD accumulation, mitochondrial dysfunction, and widespread alterations in sphingolipid metabolism. These defects compromise the structural integrity and thermosensory function of amphid neurons during early adulthood, while the capacity of SEX-1 to restrict neuronal lipid droplet accumulation declines with age. Notably, genetic modulation of sphingolipid metabolic pathways rescues neuronal defects, establishing a causal link between lipid metabolic homeostasis and neuronal maintenance. Together, our findings identify a PPARγ-like signalling axis that integrates sphingolipid metabolism, organelle quality control, and neuronal homeostasis, providing a mechanistic framework for understanding how metabolic regulation promotes neuroprotection.
    DOI:  https://doi.org/10.64898/2026.09.28.755091
  31. bioRxiv. 2026 Oct 01. pii: 2026.09.30.755414. [Epub ahead of print]
      Protein homeostasis, or proteostasis, is essential for cellular health, and its disruption contributes to cancer, aging, and neurodegenerative disease. Proteostasis is maintained largely by two intracellular degradation systems: the ubiquitin proteasome system (UPS) and the autophagy lysosomal pathway (ALP). Here, we combine pulse stable isotope labeling by amino acids in cell culture (pSILAC) with selective inhibition of the UPS or ALP to quantify pathway-dependent protein turnover and identify substrates that are preferentially cleared through each route. Direct comparison of these perturbations is complicated by their markedly different response distributions. To address the mismatch in dynamic range, we developed a normalization strategy based on within-condition ranks. Protein stabilization values are converted to percentile scores before comparison across pathways, placing both perturbations on a common relative response scale. Across two independent pSILAC experiments, 5,518 proteins were quantified in at least one condition, and 3,814 yielded high confidence half-life measurements in control, proteasome-inhibited, and lysosome-inhibited conditions. Rank normalization resolved pathway sensitivities that were obscured by direct comparison of absolute half-life changes. Importantly, the method reports relative pathway preference rather than absolute pathway contribution, exchanging effect size magnitude for comparability across perturbations with unequal response distributions. Integration with a curated proteostasis network annotation revealed coherent pathway preferences, including coordinated stabilization of proteasome core and regulatory subunits following lysosomal inhibition. This finding provides proteome-wide quantitative evidence for proteaphagy that complements previous targeted observations. Together, these results establish rank normalization as a practical strategy for comparing degradation resolved proteome turnover across perturbations with different dynamic ranges.
    DOI:  https://doi.org/10.64898/2026.09.30.755414
  32. Dev Cell. 2026 Oct 14. pii: S1534-5807(26)00350-3. [Epub ahead of print]61(10): 1941-1942
      Several intracellular regulators of stress granules (SGs) have been identified but it remains unclear whether SGs are also coordinated by extracellular signals. In this issue of Developmental Cell, Li et al. identify an extracellular nitrate-responsive module that helps assemble the SG under acute stress and later promotes its autophagic degradation.1.
    DOI:  https://doi.org/10.1016/j.devcel.2026.09.002
  33. J Adv Res. 2026 Oct 14. pii: S2090-1232(26)00782-4. [Epub ahead of print]
       BACKGROUND: Doxorubicin (DOX) is a key chemotherapeutic agent for hematologic malignancies and many solid tumors, but its clinical use is limited by doxorubicin-induced cardiotoxicity (DIC). DIC may present as subclinical myocardial injury, arrhythmias, left ventricular dysfunction, cardiomyopathy, or heart failure. DOX can disrupt organelle function through topoisomerase IIβ (Top2β)-mediated DNA damage and transcriptional stress, oxidative stress, disrupted iron homeostasis, and calcium imbalance. Mitochondrial and endoplasmic/sarcoplasmic reticulum (ER/SR) injury are therefore central pathological features of DIC.
    AIM OF REVIEW: This review summarizes current evidence on mitophagy and ER-phagy in DIC, with emphasis on discrepancies in reported findings across different experimental settings, potential crosstalk mechanisms, and the translational limitations of targeting these pathways for cardioprotection.
    KEY SCIENTIFIC CONCEPTS: Current studies suggest that mitophagy in DIC follows a checkpoint-dependent pattern. Depending on DOX dose, exposure duration, and lysosomal degradative capacity, mitophagy may remove damaged mitochondria, but it may also worsen mitochondrial injury when initiation is insufficient, activation is excessive, or flux is stalled. In contrast, direct evidence for ER-phagy in DIC remains limited. This evidence is mainly derived from CCPG1-mediated protective ER-phagy in chronic fractionated DOX models and FAM134B-associated ER-phagy-related injury signals in acute high-dose injury models. Thus, the functional divergence of ER-phagy in DIC requires confirmation in additional experimental models with rigorous autophagic flux assessment. Mitochondria-associated ER membranes (MAMs) may coordinate mitophagy and ER-phagy by regulating calcium transfer, autophagosome formation, and receptor localization. Overall, current evidence does not support indiscriminate activation or inhibition of mitophagy and ER-phagy. Instead, future interventions may need to preserve flux-complete organelle clearance while avoiding excessive or stalled autophagic signaling. In addition, this framework may help generate research hypotheses that integrate cardioprotection with preservation of antitumor efficacy. However, most evidence comes from cell and animal studies, and further validation in human myocardial tissue and confirmation of cardiac target engagement are still needed.
    Keywords:  Doxorubicin-induced cardiotoxicity; ER-phagy; Mitochondria-associated ER membranes; Mitophagy
    DOI:  https://doi.org/10.1016/j.jare.2026.10.022
  34. Pharmacol Res. 2026 Oct 14. pii: S1043-6618(26)01592-6. [Epub ahead of print]233 109677
      Lipid droplets (LDs) coordinate cellular lipid utilization, energy homeostasis, redox balance, and autophagy through dynamic inter-organelle communication with mitochondria. This review summarized recent advances in the molecular mechanisms regulating LD-mitochondria interactions and discusses how their dysregulation contributes to disease progression. Accumulating evidence has indicated that the contacts between LD and mitochondria are dynamically regulated through specialized membrane contact sites and protein complexes, such as Perilipin (PLIN) family of proteins, Mitofusin2 (Mfn2), and Rab GTPases. Rather than being a passive structural association, this interaction serves as a regulatory hub that integrates fatty acid (FA) transport, metabolic adaptation, and stress responses. It enables bidirectional regulation of lipid metabolism, allowing cells to flexibly and efficiently switch between lipid storage and FA oxidation in response to metabolic signals. Disruption of this inter-organelle communication impairs intracellular lipid utilization, compromises mitochondrial function, and exacerbates oxidative stress and ferroptosis. Such dysfunction is increasingly recognized as a core mechanism underlying metabolic disorders, cardiovascular diseases and neurodegenerative diseases. In the future, integration of protein regulation, gene editing technologies, and precision therapeutic approaches may enable specific targeting of LD-mitochondria communication, thereby offering new avenues for the treatment of relevant diseases.
    Keywords:  Cardiovascular diseases; Lipid droplet; Metabolic diseases; Mitochondria; Neurodegenerative diseases
    DOI:  https://doi.org/10.1016/j.phrs.2026.109677