bims-mecosi Biomed News
on Membrane contact sites
Issue of 2026–10–11
eight papers selected by
Verena Kohler, Umeå University



  1. Neuroscientist. 2026 Oct 07. 10738584261488785
      The neuronal endoplasmic reticulum (ER) forms a continuous membrane network that extends throughout the soma, dendrites, axons, and synaptic compartments. Although traditionally viewed as a structurally continuous intracellular organelle, recent advances in volume electron microscopy, super-resolution imaging, and live-cell functional analyses have revealed that the ER is highly compartmentalized into specialized structural and molecular domains. These domains organize local Ca2+ release, store refilling, luminal Ca2+ redistribution, and inter-organelle communication through membrane contact sites, thereby enabling the diverse physiological functions of the ER. Emerging evidence further indicates that ER topology is a fundamental determinant of diverse ER functions and that disruption of ER architecture is increasingly implicated in the pathogenesis of neurological disorders. In this review, I first summarize the ultrastructural organization of the neuronal ER based on representative electron microscopy observations and then discuss how spatial compartmentalization provides an organizational principle linking ER structure to intracellular signaling, neuronal homeostasis, and neurological disorders.
    Keywords:  Purkinje cell; calcium store; electron microscopy; endoplasmic reticulum; neuron; store-operated calcium entry
    DOI:  https://doi.org/10.1177/10738584261488785
  2. Drug Des Devel Ther. 2026 ;20 641584
      Cardiovascular diseases (CVDs) remain a leading threat to human health, imposing substantial morbidity and a considerable clinical burden worldwide. Disrupted mitochondrial calcium ions (Ca2⁺) homeostasis is increasingly recognized as a shared pathophysiological feature of diverse CVDs. Mitochondria and the endoplasmic reticulum (ER) are key organelles involved in intracellular Ca2⁺ homeostasis and energy metabolism, and their physical and functional coupling occurs at mitochondria-associated ER membranes (MAMs). Through protein complexes such as IP3R-GRP75-VDAC1, VAPB-PTPIP51 and MFN1-MFN2, MAMs coordinate a finely tuned Ca2⁺-signalling network that is essential for maintaining mitochondrial Ca2⁺ homeostasis. This review provides a systematic overview of the structural organization of MAMs and the molecular mechanisms governing MAM-mediated Ca2⁺ transfer, with particular emphasis on how dysregulated Ca2⁺ signalling at MAMs contributes to myocardial ischaemia-reperfusion injury, atherosclerosis, heart failure (HF), pulmonary arterial hypertension and diabetic cardiomyopathy. Furthermore, on this basis, this review focuses on the IP3Rs‑GRP75‑VDAC1 complex, mitochondrial calcium uniporter (MCU)‑associated calcium‑transport pathways, the endoplasmic reticulum stress‑MAMs‑mitochondrial calcium overload axis, as well as MAMs‑mediated signaling cascades, and systematically elaborates the latest research advances of therapeutic interventions including small‑molecule inhibitors, targeted peptides, calcium chelators, chemical chaperones and natural products. At present, available therapeutic evidence is mostly obtained from cellular and animal models. The process of clinical translation is still constrained by suboptimal target selectivity, dilemmas in bidirectional calcium‑signal regulation, bottlenecks in tissue‑specific delivery and the lack of long‑term safety evaluation. This review is expected to provide theoretical foundations and cutting‑edge insights for novel cardiovascular drug discovery and translational research targeting MAMs‑related calcium homeostasis.
    Keywords:  calcium homeostasis; cardiovascular diseases; mitochondria-associated endoplasmic reticulum membranes; pathophysiology; targeted therapy
    DOI:  https://doi.org/10.2147/DDDT.S641584
  3. Adv Sci (Weinh). 2026 Oct 06. e78137
      Mitochondrial transfer and transplantation (mitoTT) has emerged as an experimental and potentially transformative therapeutic strategy, drawing attention for its ability to modulate cellular bioenergetics, stress responses, and tissue repair. Endogenous mitochondrial transfer can occur through tunneling nanotubes, extracellular vesicles, cell fusion, gap junction-associated communication, and phagocytosis-like internalization. These routes differ substantially in distance, directionality, cargo integrity, regulatory control, and physiological relevance. Preclinical studies indicate that exogenous mitochondria may transiently improve bioenergetic function, attenuate oxidative stress, and support recovery in models of cardiac, skeletal muscle, and nervous system injury, whereas clinical evidence remains limited and heterogeneous. Broad clinical implementation remains constrained by unresolved biological and translational barriers. These include inefficient or poorly controlled uptake of extracellular mitochondria, uncertain long-term persistence, incomplete functional integration, donor-recipient incompatibility, mitochondrial-nuclear mismatch, heteroplasmy-related risks, immunogenicity, and the lack of standardized potency and delivery assays. Here, we critically synthesize the cellular mechanisms enabling mitoTT, emphasizing the checkpoints that determine whether transferred mitochondria are integrated, remodeled, immunologically sensed, or eliminated. We further discuss cristae biology and the mitochondrial contact site and cristae organizing system, mitochondrial nucleoid maintenance, mitochondrial DNA replication, organelle contact sites, and emerging bioengineering strategies required to move mitoTT from experimental rescue toward reproducible therapeutic application.
    Keywords:  cell metabolism; inter‐organelle contact sites; mitoTT; mitochondria; mitochondrial DNA; mitochondrial transfer; mitochondrial transplantation
    DOI:  https://doi.org/10.1002/advs.78137
  4. Neurobiol Dis. 2026 Oct 07. pii: S0969-9961(26)00388-8. [Epub ahead of print] 107642
      VPS13A belongs to the family of bridge-like lipid transfer proteins, which connect opposing membranes at organelle contact sites in order to facilitate bulk lipid transfer. Loss of function mutations in the VPS13A gene cause VPS13A disease. Diminished store operated calcium entry has previously been described in patient-derived fibroblasts and iPSC-derived neurons from VPS13A disease patients and impairments in mitochondrial calcium uptake was observed in patient-derived fibroblasts. However, how calcium (dys)homeostasis is regulated and its effects on neuronal survival remain enigmatic. Here, we investigated calcium regulation and cell death in induced pluripotent stem cell-derived neurons from VPS13A disease patients. We demonstrate that reduced store operated calcium entry is associated with diminished plasma membrane-ER contact sites and altered expression of the calcium release-activated calcium channel ORAI1. VPS13A-deficient neurons further exhibited elevated mitochondrial calcium levels, as well as resistance of the mitochondrial calcium uniporter to inhibition by Ru360. Further, VPS13A disease neurons show increased lipid peroxidation, driving ferroptotic cell death. These findings establish a mechanistic link between disrupted calcium homeostasis and neuronal degeneration in VPS13A disease and identify calcium (dys)homeostasis and ferroptosis as potential pathogenic pathways and therapeutic targets.
    DOI:  https://doi.org/10.1016/j.nbd.2026.107642
  5. J Adv Res. 2026 Oct 05. pii: S2090-1232(26)00769-1. [Epub ahead of print]
       INTRODUCTION: Hypoxia following mucosal congestion in clinical practice causes a wide range of gastrointestinal symptoms and induces profound structural and functional perturbations in mitochondria-associated ER membranes (MAMs), which are subcellular compartments whose integrity and stability are regulated by FUN14 domain-containing protein 1 (FUNDC1).
    OBJECTIVES: To investigate the effect of hypoxia-induced MAMs formation on gastric mucosal lesions in patients with severe hepatic disorders.
    METHODS: Liver cirrhosis (LC) and hepatic failure (HF) were selected as representative severe hepatic diseases, and gastric mucosal tissues were collected. We applied the gastrointestinal symptom rating scale (GSRS) and endoscopic images to evaluate the possible relationship between gastrointestinal symptoms and mucosal lesions. Portal hypertension (PHT)-induced mouse models and hypoxia-induced cell models were also established. The roles of FUNDC1, hypoxia-induced MAMs formation and mitochondrial oxidative stress in mucosal epithelial injury were analyzed.
    RESULTS: Patients with LC or HF frequently experienced gastrointestinal symptoms, which were correlated with the progression of gastric mucosal lesions. Hypoxia induced the upregulated expression of HIF-1α in gastric mucosal tissues, which was directly associated with the FUNDC1 promoter region, thereby increasing FUNDC1 gene transcription. Moreover, METTL3-mediated m6A methylation of FUNDC1 established a posttranscriptional regulatory layer to collectively drive upregulation of FUNDC1 expression. In addition, the increased level of FUNDC1 facilitated the formation of MAMs, drove a metabolic shift toward increased glycolysis, and elicited mitochondrial reactive oxygen species (mtROS) production. Ultimately, this increase in mtROS generation promoted NINJ1 oligomerization/activation to exacerbate gastric epithelial cell death and mucosal injury.
    CONCLUSION: Under hypoxic conditions, FUNDC1-regulated MAMs formation and mitochondrial oxidative stress play pivotal roles in the development of gastric mucosal lesions.
    Keywords:  FUNDC1; GSRS; Gastric mucosal lesions; Hypoxia; MAMs
    DOI:  https://doi.org/10.1016/j.jare.2026.10.007
  6. Cancer Res. 2026 Oct 08.
      Lenvatinib is the most widely used first-line treatment for advanced hepatocellular carcinoma (HCC). Nevertheless, drug resistance remains a major clinical challenge, highlighting the need to identify the underlying mechanistic drivers. Here, we identified a role for annexin A1 (ANXA1) in promoting lenvatinib resistance by supporting endoplasmic reticulum (ER)-mitochondria communication. Live-cell structured illumination microscopy revealed that ANXA1 deficiency induced the dissociation of ER-mitochondria contact sites (ERMCS), and Ca2+ kinetic analysis revealed that ANXA1 enhanced mitochondrial Ca2+ coupling. ANXA1 promoted ERMCS by directly binding the ER-mitochondria Ca2+ transfer tethers GRP75 and ITPR1 and promoting their interaction. Functionally, ANXA1 sustained oxidative phosphorylation following lenvatinib treatment and promoted cell survival. We further found that ANXA1 RNA stability was governed by an 8-oxoguanine modification-mediated ROS feedback loop. Therapeutically, photoacoustic imaging-guided in vivo analyses demonstrated that targeting this epigenetic-organelle communication feedback loop resensitized HCC to lenvatinib treatment, inhibiting peritumoral angiogenesis and improving the intratumoral hypoxic microenvironment. These findings uncover ERMCS formation as a driver of lenvatinib resistance in HCC, establishing a potential therapeutic strategy for targeting organelle communication to reverse drug resistance.
    DOI:  https://doi.org/10.1158/0008-5472.CAN-26-2074
  7. J Cell Sci. 2026 Oct 01. pii: jcs264817. [Epub ahead of print]139(19):
      The endoplasmic reticulum (ER) is the gateway to the eukaryotic protein secretory pathway. Beyond its role in protein biogenesis, it is central to Ca2+ homeostasis and lipid biosynthesis. This organelle, which can constitute more than 50% of the cellular membranes in secretory cells, is highly plastic and must adjust to intracellular or extracellular challenges to ensure proper protein secretion. ER stress, resulting from challenges such as accumulation, misfolding or aggregation of proteins or from disrupted ER lipid composition, can deleteriously affect cell function. Thus, the ER has evolved adaptive mechanisms that lead to cellular reprogramming to adjust its capacity to handle stress, including the unfolded protein response (UPR), which engages various ER quality control systems, protein degradation pathways and ER-organelle contacts. If this succeeds, the cell survives; but if it fails, cell death mechanisms are triggered. In this Cell Science at a Glance article and the accompanying poster, we summarize current knowledge on ER stress and control of the UPR in mammalian cells, highlighting aspects that require further attention. We also discuss recent insights that must be considered to better capture the full understanding of the ability of the ER to adjust to biological variation.
    Keywords:  Contact sites; Endoplasmic reticulum; Proteostasis; UPR; Unfolded protein response
    DOI:  https://doi.org/10.1242/jcs.264817
  8. Biophys J. 2026 Oct 06. pii: S0006-3495(26)00694-6. [Epub ahead of print]
      The endoplasmic reticulum (ER) is the largest continuous membrane-bound organelle in the cell and plays a central role in the synthesis and turnover of lipids and proteins. It connects directly to the nucleus through specialized contact sites known as ER-nuclear envelope (NE) junctions. In a recent study, we showed that these junctions are sparse and highly constricted, measuring less than 20 nm in diameter and occurring at a frequency of approximately 0.1 junctions per square micrometer. However, it remains unclear whether such limited and narrow connections are sufficient to support efficient transport between the ER and NE. Here, we developed a mathematical model of ER-to-NE protein diffusion that incorporates ultrastructural parameters of ER-NE junctions, their spatial frequency, and protein diffusion coefficients within the ER lumen. To validate the model, we experimentally quantified the mobility of ER luminal proteins to the NE using fluorescence recovery after photobleaching (FRAP). Both the model and experimental measurements demonstrate that passive diffusion is sufficient to account for rapid protein exchange between the ER and NE despite the sparse and constricted nature of ER-NE junctions. Furthermore, the model predicts how junction geometry and abundance influence transport efficiency. Together, these findings provide a quantitative framework for understanding ER-NE connectivity and establish that simple diffusion can account for efficient protein transport between the ER and nucleus.
    Keywords:  continuum equations; kinetic equations; mean-field limit
    DOI:  https://doi.org/10.1016/j.bpj.2026.10.002