bims-mecosi 2026-08-02 papers

bims-mecosi

Biomed News

on Membrane contact sites

Issue of 2026–08–02
thirteen papers selected by
Verena Kohler, Umeå University

Structural Organization of the Nvj3-Mdm1 Complex Reveals a Conserved Lipid-Compatible Contact Site Module.
Vimentin intermediate filaments support autophagosome biogenesis at ER-endosome contact sites in response to starvation.
SGLT2 Inhibitors as Modulators of Mitochondrial Ion Transport and ER-Mitochondria Crosstalk in Diabetic Cardiomyopathy.
Approaches to Organelle Spacing at Membrane Contact Sites.
Nanoscale biointerfaces in inter-organelle communication: membrane contact sites, organelle trafficking, and cell fate control.
ATL2 Recruits TRAK1 to Promote Mitochondrial Transport at ER-Mitochondria Contact Sites.
Rabs in the driving seat: Coordinating vesicular traffic and membrane contact site dynamics.
The endo-lysosomal-lipid axis: bidirectional interactions between membrane trafficking dysfunction and lipid metabolic disorders.
Estrogen attenuates sepsis-induced renal vascular dysfunction in rats: Correlation with preservation of mitochondria-associated ER membranes.
Integrative structure determination of a human mitochondrial contact site and cristae organizing system (MICOS) sub-assembly.
Research Progress on Downstream Mechanisms of Glucose Metabolic Reprogramming and Its Role in the Occurrence and Progression of Type 2 Diabetes Mellitus.
Spatial control of mitochondrial retrograde signaling by nuclear pore-associated contact sites.
Intermembrane coupling between Bcl-xL and the IP3 receptor supports local Ca2+ transfer at ER-mitochondrial contacts.

Contact (Thousand Oaks). 2026 Jan-Dec;9:9 25152564261471395

Structural Organization of the Nvj3-Mdm1 Complex Reveals a Conserved Lipid-Compatible Contact Site Module.

Marwa Aboumourad, Hanaa Hariri.

  Membrane contact sites are organized by protein assemblies that physically couple organelles and coordinate lipid metabolism, yet the structural principles that enable lipid exchange across these junctions remain poorly defined. At the nuclear-vacuolar junction (NVJ) in budding yeast, the tethering protein Mdm1 and its binding partner Nvj3 form a complex that regulates lipid metabolic pathways, but the structural features underlying their interaction have not been resolved. Here, we use AlphaFold-based complex prediction and comparative structural analysis to define the organization of Nvj3-Mdm1 complex assembly. We identify a high-confidence heterodimer in which conserved PXA and PXC domains generate an extended tunnel spanning both proteins. Tunnel analysis predicts a core hydrophobic conduit traversing the Nvj3-Mdm1 interface, consistent with a lipid-compatible architecture. Evolutionary conservation is enriched at the Nvj3-Mdm1 interface. The predicted conduit shares geometric and physicochemical properties with bridge-like lipid transfer proteins, including Atg2, Fmp27, and Hob2, suggesting that heteromeric tether assemblies may contribute directly to inter-organelle lipid transfer. Notably, this conduit is predicted to arise from a heteromeric α-helical assembly rather than the β-sheet-rich architecture characteristic of canonical bridge-like lipid transfer proteins. Comparative phylogenetic analyses showed that Nvj3 and Mdm1 share broadly congruent evolutionary patterns across Saccharomycetes, consistent with their conserved functional association. Together, these findings define Nvj3 as a structural partner of Mdm1 and support a conduit-based model of lipid transfer at the NVJ.

Keywords:  SNX-RGS; alphafold; coevolution; lipid transfer protein (LTP); membrane contact sites; nuclear ER-vacuole junction; structural prediction; tether

DOI:  https://doi.org/10.1177/25152564261471395
J Cell Sci. 2026 Jul 15. pii: jcs264635. [Epub ahead of print]139(14):

Vimentin intermediate filaments support autophagosome biogenesis at ER-endosome contact sites in response to starvation.

Quentin Frenger, Dobrawa Amiri Czajkowski, Carla Alemany, Damiana Lecoeuche, Cédric Delevoye, Etienne Morel.

  Macroautophagy (autophagy) is a fundamental catabolic process requiring the biogenesis of the autophagosome to support cell survival during stress. Although the roles of F-actin and microtubule cytoskeleton in autophagy are well established, the contribution of intermediate filaments (IFs) remains poorly understood. Here, we investigated the role of the type III IF vimentin in supporting the early steps of starvation-induced autophagy. We demonstrate that starvation triggers a rapid, perinuclear compaction of vimentin IFs, which showed enhanced overlap with the endoplasmic reticulum (ER) and correlated with transient vimentin phosphorylation at serine 56. We reveal that autophagic proteins accumulate at the vimentin-ER interface, physically connecting the autophagosome biogenesis machinery to the vimentin IF network. Knockout or pharmacological perturbation of vimentin-IFs dynamics using withaferin-A significantly impairs starvation-induced autophagic flux. Mechanistically, we reveal that vimentin IFs are essential coordinators for the mobilization of endosome-ER membrane contact sites (EERCS), a crucial hub for autophagosome nucleation. Together, our findings uncover a novel role for vimentin IFs as a dynamic cytoskeletal coordinator that spatially organizes membrane contact sites to promote the efficient initiation of autophagosome biogenesis in response to nutrient stress.

Keywords:  Autophagosome; Autophagy; Endoplasmic reticulum; Intermediate filaments; Membrane contact sites; Vimentin

DOI:  https://doi.org/10.1242/jcs.264635
Am J Physiol Cell Physiol. 2026 Jul 29.

SGLT2 Inhibitors as Modulators of Mitochondrial Ion Transport and ER-Mitochondria Crosstalk in Diabetic Cardiomyopathy.

Jessa Flores, Maria Victoria Faith Garcia, Prycelline Abedejos, Jed Allyn Hernandez, Trong Kha Pham, Hyoung Kyu Kim, Jubert Marquez, Jin Han.

  Diabetic cardiomyopathy (DCM) is a major complication of type 2 diabetes mellitus and a leading contributor to heart failure. A central feature of DCM is the disruption of mitochondrial bioenergetics and calcium homeostasis, processes that are tightly regulated through mitochondria-associated endoplasmic reticulum membranes (MAMs). These ER-mitochondria contact sites coordinate mitochondrial ion transport systems, including the mitochondrial calcium uniporter (MCU), Na⁺/Ca²⁺ exchanger (NCLX), and potassium channels, which collectively govern mitochondrial metabolism, redox balance, and cell survival.

Keywords:  diabetic cardiomyopathy; endoplasmic reticulum stress; mitochondria; mitochondrial channels; type 2 diabetes mellitus

DOI:  https://doi.org/10.1152/ajpcell.00230.2026
Contact (Thousand Oaks). 2026 Jan-Dec;9:9 25152564261473365

Approaches to Organelle Spacing at Membrane Contact Sites.

Tomas Knedlik, Federica Dal Bello, Marta Giacomello.

  Membrane contact sites (MCSs) are points where organelle surfaces are juxtaposed, without fusion of their membranes. Research in the MCS field has widely focused on the molecules and mechanisms that hold organelles together, known as "tethers", based on the correct presumption that processes mediated by MCSs depend on their spatial proximity. However, it has become clear that the distance between the membranes also have a biological role, particularly in processes such as Ca2+ transfer, while its relevance for other functions, such as lipid exchange, remains less clear. This supports the idea that there may be molecules that keep membranes apart, referred to as "spacers". While some evidence supports this hypothesis, the mechanisms of spacing remain unclear. In this opinion article, we briefly describe three potential spacing mechanisms that we have hypothesised based on direct and indirect experimental evidence. Briefly, we propose the existence of different types of organelle spacing approaches (OSAs) that result in organelle distancing: first, the presence of rod-like spacing molecules; second, the removal of some tethers, achieved through their masking, dissociation from MCSs, or degradation, which could result either in complete untethering of the organelles or in variations in the distance between them due to changes in the composition of the MCSs; third, cytoskeleton-mediated pulling forces that can increase the distance between the two apposing membranes. Our aim is to stimulate discussion and initiate debate on the importance of maintaining the correct distance between organelles.

Keywords:  contact; membrane; organelle; signaling(signalling); tether

DOI:  https://doi.org/10.1177/25152564261473365
Front Cell Dev Biol. 2026 ;14 1901757

Nanoscale biointerfaces in inter-organelle communication: membrane contact sites, organelle trafficking, and cell fate control.

Mohamed R Abdel-Hamed, Sameh Saber, Elsayed A Elmorsy, Basem H Elesawy, Maha M Amer, Abdel-Moneim Hafez Abdel-Moneim, Alaa El-Din L Firgany, Enas A Mohamed, Huda Eltayeb, Ageeb M Hassan, Mohamed El-Sayed, Ahmed Y Kira.

  Cellular and tissue organization depends on the spatial arrangement, ultrastructure, and functional coupling of organelles. This review reframes intracellular nanomaterials as nanoscale tools for interrogating and modulating membrane contact sites (MCSs), rather than simply as delivery systems. We focus on mitochondria, the endoplasmic reticulum, lysosomes, endosomes, and the nucleus because these compartments form dynamic contact networks that regulate metabolism, calcium and redox signaling, membrane trafficking, autophagy, mitophagy, chromatin organization, stress adaptation, and cell fate. Emphasis is placed on morphological and ultrastructural readouts, including mitochondrial cristae organization, fission-fusion balance, membrane-potential-dependent localization, endosomal and lysosomal trafficking, ER-mitochondria and lysosome-mitochondria communication, nuclear-pore access, chromatin organization, and inter-organelle contact-site remodeling. We discuss how particle size, surface charge, geometry, ligand presentation, and stimulus-responsive behavior influence cellular uptake, endosomal escape, organelle localization, and structural consequences within cells and tissues. A central distinction is made between intentional organelle nano-regulation, in which engineered systems are designed to engage defined subcellular mechanisms and organelle interfaces, and incidental stress responses, in which altered morphology or gene expression reflects oxidative, lysosomal, mitochondrial, inflammatory, or genotoxic injury. By organizing current evidence around MCS biology, subcellular compartmentalization, membrane trafficking, organelle dynamics, and tissue-relevant cell fate decisions, this review provides a morphology-centered framework for evaluating intracellular nanomaterials in health, disease, stem-cell biology, and regenerative bioengineering.

Keywords:  ER–mitochondria crosstalk; cell fate regulation; endolysosomal trafficking; inter-organelle communication; membrane contact sites; organelle-targeted nanomaterials

DOI:  https://doi.org/10.3389/fcell.2026.1901757
Adv Sci (Weinh). 2026 Jul 30. e76972

ATL2 Recruits TRAK1 to Promote Mitochondrial Transport at ER-Mitochondria Contact Sites.

Yiru Cheng, Peiyuan Chai, Xiayuhe Pei, Yiwen Chen, Xiaoshuai Huang, Bei Liu, Yiqian Wu, Junlin Teng, Pengli Zheng, Jianguo Chen.

  Mitochondrial transport and distribution are crucial for cellular homeostasis, yet whether and how they are regulated by endoplasmic reticulum (ER)-mitochondria contact sites remains unclear. Here, we demonstrate that the ER protein atlastin-2 (ATL2) orchestrates mitochondrial transport and distribution by promoting assembly of the transport machinery at ER-mitochondria contact sites. Mechanistically, ATL2 recruits the adaptor trafficking kinesin-binding protein 1 (TRAK1) to the ER membrane, strengthening the interaction of TRAK1 with the mitochondrial transport adaptor MIRO1 to promote anterograde mitochondrial transport. Loss of ATL2 disrupts this process, leading to perinuclear mitochondrial clustering. We further find that ATL2 stabilizes ER-mitochondria contact sites by interacting with MFN2, providing a platform for mitochondrial transport complex assembly. Moreover, in hypoxia, ATL2 is ubiquitinated at lysine 567 by the E3 ligase SYVN1, leading to its degradation and a resulting defect in mitochondrial distribution. Our findings elucidate a novel ER-mediated mechanism for mitochondrial transport.

Keywords:  ATL2; ER–mitochondria contact sites; TRAK1; hypoxia; mitochondrial transport

DOI:  https://doi.org/10.1002/advs.76972
Curr Opin Cell Biol. 2026 Jul 30. pii: S0955-0674(26)00065-7. [Epub ahead of print]102 102677

Rabs in the driving seat: Coordinating vesicular traffic and membrane contact site dynamics.

Yogita Phogat, Sankalita Paul, Mahak Sharma.

Rab GTPases are central regulators of intracellular membrane organization, ensuring the specificity and directionality of vesicular transport. Operating as 'molecular switches,' Rab GTPases cycle between an active GTP-bound and an inactive GDP-bound state, a process regulated by GEFs (guanine nucleotide exchange factors) and GAPs (GTPase-activating proteins). The dynamic switch-like behaviour and compartment-specific localization of Rab GTPases establish membrane identity and generate discrete membrane subdomains, providing spatiotemporal control over intracellular trafficking events. Rab GTPases also facilitate compartment maturation through coordinated Rab conversion, leading to transitions between different membrane identities. Membrane-localized Rab GTPases function as a recruitment platform for a cohort of effector proteins, which regulate the sequential steps of vesicular transport. The features discussed above also enable Rabs to participate in the formation of membrane contact sites, which facilitate direct transport of phospholipids and small molecules between compartments and regulate organelle motility and positioning. Here we review current insights into the mechanisms governing Rab GTPase regulation, including post translational modifications and interactions with effectors. We also discuss their roles in membrane domain formation, compartment maturation via Rab cascades, and non-vesicular communication pathways. These findings enhance our understanding of the multifaceted functions of Rab GTPases in compartmentalization and highlight emerging areas for future investigation.

DOI: https://doi.org/10.1016/j.ceb.2026.102677
Front Cell Dev Biol. 2026 ;14 1860821

The endo-lysosomal-lipid axis: bidirectional interactions between membrane trafficking dysfunction and lipid metabolic disorders.

Yao Du, Li Li, Mingtao Du, Zhi Xu, Xiaorong Zhang, Wa Cao.

  The endo-lysosomal system is a central regulator of intracellular trafficking, cargo degradation, and metabolic homeostasis. Its dynamic function is closely intertwined with lipid metabolism, forming an integrated regulatory network termed the endo-lysosomal-lipid axis. Disruption of this axis can impair endosomal maturation, lysosomal acidification, autophagic degradation, and lysosome-centered signaling pathways, resulting in defective cellular clearance and chronic inflammatory responses. Conversely, dysfunction of the endo-lysosomal system disrupts cholesterol trafficking, lipid redistribution, and macromolecular degradation, ultimately promoting secondary lipid accumulation and metabolic imbalance. In this review, we summarize the reciprocal interactions between lipid metabolism and endo-lysosomal function, with particular emphasis on membrane trafficking, lysosomal homeostasis, autophagy, membrane contact sites, and multicellular lipid clearance networks. We further discuss how these interconnected processes contribute to disease progression and highlight emerging therapeutic strategies aimed at restoring lysosomal function and lipid homeostasis. Understanding the dynamic regulation of the endo-lysosomal-lipid axis may provide new mechanistic insights into metabolic and neurodegenerative disorders and identify novel therapeutic opportunities.

Keywords:  autophagy; cholesterol trafficking; endo-lysosomal system; endo-lysosomal–lipid axis; lipid metabolism; lysosomal dysfunction; metabolic disease

DOI:  https://doi.org/10.3389/fcell.2026.1860821
Life Sci. 2026 Jul 27. pii: S0024-3205(26)00412-1. [Epub ahead of print]402 124603

Estrogen attenuates sepsis-induced renal vascular dysfunction in rats: Correlation with preservation of mitochondria-associated ER membranes.

Min Xi, Jing Wang, Xiao-Qi Yue, Yang Yang, Yu-Ping Zhang, Si-Jie Chen, Zhen-Ao Zhao, Sheng-Jun Liu, Chun-Yu Niu, Zi-Gang Zhao.

   AIMS: To determine whether estrogen (E2) protects against sepsis-induced renal vascular dysfunction and whether this effect is associated with preservation of mitochondria-associated endoplasmic reticulum membrane (MAM) in rats.
MATERIALS AND METHODS: Male Wistar rats were randomly assigned to Sham, Sham+E2, Sepsis, and Sepsis+E2 groups. Sepsis was induced by intraperitoneal injection of allogeneic fecal filtrates (FF, 1 g/kg), and E2 (2 mg/kg) was administered intramuscularly 1 h after FF or vehicle injection. Renal vascular resistance (RI), peak systolic velocity (PSV), mean arterial pressure (MAP), and heart rate (HR) were measured. Serum creatinine (SCr), blood urea nitrogen (BUN), renal blood perfusion, isolated renal artery reactivity, MAM ultrastructure, and IP3R1 and VDAC1 expressions were assessed.
KEY FINDINGS: E2 treatment significantly improved 72 h survival, general condition, MAP, and HR in septic rats, attenuated sepsis-induced increases in SCr and BUN, reduced renal histopathological damage, and ameliorated renal blood perfusion. E2 decreased RI and PSV and restored norepinephrine-induced vasoconstriction and acetylcholine-induced endothelium-dependent vasodilation. Furthermore, E2 reversed sepsis-induced MAM abnormalities (decreased contact distance and increased ER-mitochondria contact coefficient) in both vascular smooth muscle and endothelial cells and normalized the sepsis-induced upregulation of IP3R1 and VDAC1 in both renal tissues and arteries.
SIGNIFICANCE: E2 attenuates sepsis-induced renal vascular dysfunction, which correlates with preservation of MAM ultrastructure and normalization of IP3R1 and VDAC1 expression in renal vascular cells. These findings identify MAM as a potential subcellular hub associated with estrogen-mediated vascular protection and provide a foundation for future mechanistic studies to define whether MAM directly contributes to these effects.

Keywords:  Acute kidney injury; Estrogen; Mitochondria-associated endoplasmic reticulum membrane; Renal vascular dysfunction; Sepsis

DOI:  https://doi.org/10.1016/j.lfs.2026.124603
bioRxiv. 2026 Jul 22. pii: 2026.07.19.739404. [Epub ahead of print]

Integrative structure determination of a human mitochondrial contact site and cristae organizing system (MICOS) sub-assembly.

Muskaan Jindal, Rakesh Mahato, Sreemoyee Das, Arko Guha, Kartik Majila, Shreyas Arvindekar, Anand T Vaidya, Shruthi Viswanath.

The Mi tochondrial contact site and C ristae O rganizing S ystem (MICOS) complex is an inner mitochondrial membrane (IMM) assembly present at the cristae junction. It is responsible for regulating cristae formation and remodeling. However, its structure is not known. We applied Bayesian integrative structure determination to characterize the structure of the Mic60, Mic19, Mic10, and Mic13-containing MICOS complex combining AlphaFold predictions with data from crosslinking mass spectrometry, biochemical assays, electron tomography, homology modeling, and sequence alignments. The integrative structure revealed novel mutual interfaces among Mic10 N,C , Mic60 LBS1,LBS2,mitofilin , and Mic13 central,C , which were experimentally validated. Several likely-pathogenic missense mutations also localize to these novel interfaces, highlighting their importance. Our results indicate that Mic13 likely facilitates MICOS assembly by binding Mic10 in the IMM-proximal region and Mic60 in the intermembrane space. Taken together, our integrative approach sheds light on the structure and assembly of the MICOS complex.

DOI: https://doi.org/10.64898/2026.07.19.739404
Biomedicines. 2026 Jun 24. pii: 1427. [Epub ahead of print]14(7):

Research Progress on Downstream Mechanisms of Glucose Metabolic Reprogramming and Its Role in the Occurrence and Progression of Type 2 Diabetes Mellitus.

Chan Wu, Maoying Wei, Aijing Li, Qingyi Zhu, Jingyi Guo, Anning Sun, Xin Gu, Yincheng Li, Yanbing Gong.

  Type 2 diabetes mellitus (T2DM) is a highly prevalent and devastating chronic metabolic disease worldwide, with pathogenesis centrally characterized by insulin resistance and pancreatic β-cell dysfunction. Accumulating evidence has demonstrated that glucose metabolic reprogramming represents an adaptive metabolic shift from oxidative phosphorylation to aerobic glycolysis in cells in response to a hyperglycemic microenvironment. This shift acts as an upstream important event driving the initiation and progression of T2DM. This review summarizes the characteristics of glucose metabolic reprogramming in insulin-sensitive target organs under T2DM conditions, including the liver, skeletal muscle, adipose tissue and pancreatic β-cells. It also discusses four major downstream effector mechanisms: mitochondrial energy metabolism disturbance, augmented oxidative stress, disruption of mitochondria-associated endoplasmic reticulum membranes (MAMs) coupled with calcium homeostasis imbalance, and systemic inflammatory response. On this basis, we summarize the intervention strategies targeting the above signaling pathways, including antioxidant therapy, restoration of MAMs integrity and calcium homeostasis, systemic anti-inflammatory intervention, and multi-target regulatory effects of traditional Chinese medicine. Current studies indicate that early intervention in downstream stress events is induced by glucose metabolic reprogramming. This is particularly true for the preservation of MAMs' integrity; restoration of calcium homeostasis; and inhibition of NLRP3 inflammasome activation, the latter of which is expected to block or delay the progression from prediabetes to clinical T2DM. Nevertheless, substantial gaps still remain in the understanding of the dynamic regulatory mechanisms of MAMs, tissue-specific therapeutic targets, and relevant clinical translational research. Future integration of multi-omics technologies will provide novel therapeutic strategies and theoretical foundations for the early prevention and treatment of T2DM.

Keywords:  glucose metabolic reprogramming; insulin resistance; mitochondria-associated endoplasmic reticulum membranes; oxidative stress; type 2 diabetes mellitus

DOI:  https://doi.org/10.3390/biomedicines14071427
bioRxiv. 2026 Jul 24. pii: 2026.07.23.740218. [Epub ahead of print]

Spatial control of mitochondrial retrograde signaling by nuclear pore-associated contact sites.

Sahana Mitra, Giulia Burrone, Surya Rubarajan, Christophe Klein, Tyler Kwok, Suchit Gutta, Keyu Chloe Li, Elizaveta Berson, Joseph Orofino, Maria Dafne Cardamone, Michael Blower, Valentina Perissi.

Mitochondria relay their functional state to the nucleus via retrograde signaling, yet whether the spatial organization of the mitochondrial network plays a role in this process remains unclear. Here, we show that stress-induced clustering of mitochondria around the nucleus is a crucial part of the retrograde response. Perinuclear clustering facilitates the formation of mitochondria- nucleus contact sites (MNCS) and the nuclear entry of GPS2, a key mediator of mitochondrial retrograde signaling essential for activating nuclear-encoded mitochondrial and stress-response genes in response to various mitochondrial stressors. Unexpectedly, TSPO-driven MNCS are dispensable for GPS2-based retrograde signaling. Instead, we identify the mitochondrial import receptor TOMM70 and the nucleoporin RanBP2/NUP358 as components of a stress-induced nuclear pore-associated tethering complex required for promoting GPS2 nuclear translocation and activation of downstream programs. These findings establish MNCS as a functional gateway for mitochondrial retrograde signaling, highlighting that organelle positioning and tethering at the nuclear pore provide an unexpected layer of stress regulation.

DOI: https://doi.org/10.64898/2026.07.23.740218
Cell Rep. 2026 Jul 30. pii: S2211-1247(26)00845-4. [Epub ahead of print]45(8): 117767

Intermembrane coupling between Bcl-xL and the IP3 receptor supports local Ca2+ transfer at ER-mitochondrial contacts.

Arijita Ghosh, David Weaver, Chi Li, Gyӧrgy Hajnóczky.

  Bcl-xL, an anti-apoptotic Bcl-2 family protein, engages laterally with Bak/Bax in the outer mitochondrial membrane (OMM) to inhibit apoptosis and interacts with the IP3 receptor Ca2+ channels (IP3Rs) in the endoplasmic reticulum (ER) membrane to control Ca2+ release. It is unknown if OMM-localized Bcl-xL can also interact in trans with IP3Rs at ER-mitochondrial contacts to form a tethering complex that supports IP3R-mediated local Ca2+ transfer from ER to mitochondria. We establish that IP3R-mitochondria Ca2+ signal propagation depends on Bcl-xL. By targeting Bcl-xL specifically to different subcellular compartments, we find that OMM-localized Bcl-xL increases the efficacy of ER-mitochondrial Ca2+ transfer without changing ER Ca2+ release, despite attenuating mitochondrial Ca2+ uptake. We find interaction between Bcl-xL and each IP3R isoform occurring at the mitochondria and a complex formed by OMM-localized Bcl-xL and IP3Rs. OMM Bcl-xL interacts with IP3Rs in trans at ER-mitochondrial contacts to optimize local Ca2+ signal propagation into the mitochondria.

Keywords:  Bcl-xL; CP: cell biology; CP: metabolism; ERMC; IP3R; calcium signaling; endoplasmic reticulum; local Ca(2+) transfer; mitochondria; organellar crosstalk

DOI:  https://doi.org/10.1016/j.celrep.2026.117767