bims-mecosi Biomed News
on Membrane contact sites
Issue of 2026–05–17
twelve papers selected by
Verena Kohler, Umeå University



  1. J Nutr. 2026 May 08. pii: S0022-3166(26)00238-5. [Epub ahead of print] 101589
      The mitochondrial-associated endoplasmic reticulum membrane (MAM) is a dynamic contact site formed through protein-mediated connections between the endoplasmic reticulum (ER) and outer mitochondrial membrane. As a pivotal signaling and metabolic hub, MAM regulates core cellular physiological processes, including calcium homeostasis, lipid biosynthesis and trafficking, mitochondrial dynamics, autophagy, apoptosis, and inflammasome formation and activation. Growing evidence indicates that the disruption of MAM integrity and function is closely associated with various disorders induced by excessive salt consumption. High salt intake perturbs ER-mitochondrial calcium ion exchange, partly through elevated intracellular sodium concentrations, leading to the structural and functional impairment of MAM. This disruption of calcium homeostasis subsequently triggers the ER and oxidative stress responses, exacerbating cellular damage. Concurrently, high-salt diets interfere with MAM-mediated lipid synthesis and transport, contributing to mitochondrial dysfunction and accelerating disease development. This review summarizes the involvement and underlying molecular mechanisms of MAM in high-salt diet-related disorders including hypertension, cardiovascular disease, obesity, and metabolic dysfunction-associated fatty liver disease. Furthermore, this review explores the translational potential of targeting MAM as a therapeutic intervention, providing novel insights for developing interventions that target inter-organelle communication to combat salt-related systemic disorders.
    Keywords:  calcium homeostasis; high-salt diet; lipid metabolism; metabolic disease; mitochondria-associated endoplasmic reticulum membrane
    DOI:  https://doi.org/10.1016/j.tjnut.2026.101589
  2. J Biol Chem. 2026 May 13. pii: S0021-9258(26)02016-8. [Epub ahead of print] 113144
      The endoplasmic reticulum (ER) is a highly dynamic intracellular organelle that forms close contact sites with other organelles and the plasma membrane. These membrane contact sites play essential roles in lipid exchange and calcium homeostasis. ER membrane proteins from the VAP, ORP, and ESYT families are key players in the formation and function of these contacts. Numerous interactions between these proteins are likely critical for their activity. We investigate the interactome between these protein families in live cells by analyzing two members from each family, using Förster Resonance Energy Transfer (FRET) between pairs of proteins labeled with fluorescent proteins (FP). FRET is detected by Fluorescence Lifetime Imaging Microscopy (FLIM). Our quantitative approach shows that all tested proteins clusterize and sometimes interact within their respective families, and that their organization at the nanometer scale can be disrupted by specific mutations or domain deletions. In particular, we show that the coiled-coil domains of ORP5 and ORP8 are required for the formation of both homomeric and heteromeric complexes. Moreover, we demonstrate that FRET-FLIM can detect intra-molecular conformational changes in response to alterations in the cellular environment, such as variations in Ca2+ concentration, as observed for ESYT1. We also identify novel inter-family organization, including clustering between VAPB and ORP8, and between ESYT2 and ORP5/8. Finally, our approach highlights the broad interaction network (interactome) of VAPA/B, and shows how various potential binding partners can influence FRET efficiency.
    Keywords:  Endoplasmic Reticulum; Extended Synaptotagmin; FRET FLIM microscopy; Membrane Contact Sites; Oxysterol-binding protein-Related Proteins; Vesicle-Associated membrane protein-associated Proteins; live-cell imaging; protein interactions
    DOI:  https://doi.org/10.1016/j.jbc.2026.113144
  3. Contact (Thousand Oaks). 2026 Jan-Dec;9:9 25152564261451671
      Autophagosome biogenesis is a highly coordinated membrane remodeling process that relies on the de novo formation and expansion of the phagophore, yet the cellular principles governing its spatial and temporal organization remain incompletely understood. Accumulating evidence now places the endoplasmic reticulum (ER) at the center of this process, not merely as a membrane source, but as a dynamic scaffold that organizes phagophore assembly through extensive membrane contact sites with multiple organelles. ER-mediated contacts with endosomes, mitochondria, the plasma membrane, and ER-Golgi intermediates create specialized microenvironments that integrate signaling, lipid transfer, vesicle formation and trafficking, and biophysical constraints to drive phagophore nucleation and growth. These contact sites enable the coordinated mobilization of diverse membrane carriers and autophagy regulators in a stress- and context-dependent manner. In this review, we discuss how ER-driven membrane contact sites orchestrate autophagosome biogenesis, highlight emerging mechanistic and biophysical concepts, and consider their broader implications for cellular stress adaptation and disease.
    Keywords:  ER-contact sites; autophagosome biogenesis; lipid transfer proteins
    DOI:  https://doi.org/10.1177/25152564261451671
  4. STAR Protoc. 2026 May 11. pii: S2666-1667(26)00216-9. [Epub ahead of print]7(2): 104563
      Endosome-endoplasmic reticulum contact sites (EERCS) are highly dynamic membrane interfaces that regulate trafficking and signaling, yet biochemical approaches to isolate them remain nonexistent, unlike established protocols for other types of contacts. Here, we present a protocol to isolate and purify endosomal membranes associated with endoplasmic reticulum membranes from cultured mammalian cells using subcellular fractionation and a two-step density-gradient centrifugation. We describe steps for cell expansion, post-nuclear supernatant collection, and the isolation of light membranes and EERCS. For complete details on the use and execution of this protocol, please refer to Da Graça et al.1.
    Keywords:  Cell Biology; Cell Membrane; Cell separation/fractionation
    DOI:  https://doi.org/10.1016/j.xpro.2026.104563
  5. Cell Mol Life Sci. 2026 May 12. pii: 207. [Epub ahead of print]83(1):
      Peroxisomes are small, highly dynamic organelles involved in a plethora of metabolic pathways. They are essential for the efficient exchange of metabolites and cellular messengers orchestrating intracellular signaling. Calcium (Ca2+) is one of the most prominent physiological signaling elements and regulates a wide variety of processes in cellular homeostasis and function. Recently, we showed that peroxisomes participate in cellular Ca2+ dynamics by taking up and releasing Ca2+ following store-operated calcium entry (SOCE), however, the mechanism of peroxisomal Ca2+ uptake and its modulators remained unknown. Using live cell imaging in combination with genetically encoded calcium indicators (GECI), we show that peroxisomal calcium dynamics are independent of PEX11β and the pore protein PXMP2. Instead, we find that the ACBD5-dependent membrane contact site between peroxisomes and the endoplasmic reticulum (ER) is necessary for efficient peroxisomal Ca2+ uptake. Further, we identify the ACBD5-dependent peroxisome-ER contact site as the major factor restricting peroxisome motility within the cell. Microtubules and SOCE stimulation exert smaller and independent effects on peroxisome motility. This work expands the range of known functions of the peroxisome-ER contact site.
    Keywords:  Calcium signaling; FRET sensor; MCS; Membrane contact site; Peroxisomal disorders
    DOI:  https://doi.org/10.1007/s00018-026-06191-4
  6. Virology. 2026 Apr 29. pii: S0042-6822(26)00145-5. [Epub ahead of print]621 110930
      Positive-sense (+)RNA viruses are major pathogens of humans, animals and plants. This review summarizes the complex subversion of the host phosphoinositide cycles for virus replication. Phosphoinositides (PIPs) are generated by tightly regulated activity of dedicated PIP kinases from PI in different subcellular locations. Phosphoinositides frequently act as molecular switches and are master regulators of membrane dynamics. Phosphoinositides are exploited by (+)RNA viruses to build membrane-associated viral RNA replication machinery called viral replication organelles (VROs) inside the infected cells. Recent discoveries with +RNA viruses demonstrated the exploitation of two phosphoinositides, PI3P and PI4P, which will be the focus in this review. Selected + RNA viruses exploit PI4P to drive nonvesicular lipid transport via counter transport of sterols and phosphatidylserine from the ER to the VRO through membrane contact sites (MCSs) and lipid transport proteins. The co-opted PI4P and PI4K kinases regulate and maintain the lipid composition of VROs during virus replication. The common strategy of exploiting PI4P and PI4K and co-opted conserved host factors involved in PI4P cycle, such as OSBP-like proteins, opens up new avenues for broad-range antiviral approaches. Several + RNA viruses exploit PI3P cycle to hijack different set of effectors and organelles or pathways to support replication. Enrichment of either PI4P or PI3P in VRO membranes leads to protective environment for RNA replication. Overall, exploitation of PI3P and PI4P phosphoinositides, which are exclusively present in different membrane microdomains, allows viruses to gain access to different resources in the host cell membranes and to regulate spatiotemporally cellular pathways and antiviral responses.
    Keywords:  Enteroviruses; Hepatitis C; Host factor; Human virus; Lipid transfer protein; Membrane contact site; PI3P; PI4P; Phosphoinositides; Replication; Tomato bushy stunt virus; Virus-host interaction
    DOI:  https://doi.org/10.1016/j.virol.2026.110930
  7. Mech Ageing Dev. 2026 May 08. pii: S0047-6374(26)00043-6. [Epub ahead of print]231 112191
      Mitochondria-lysosome contacts (MLCs) are emerging as a dynamic membrane interface that integrates organelle communication with cellular homeostasis. Rather than acting solely as intermediates of degradative trafficking, MLCs organize local calcium transfer, lipid exchange, Rab7-dependent contact remodeling, and mitochondrial quality control. These functions place MLCs at the intersection of mitochondrial fitness, lysosomal competence, metabolic adaptation, and stress signaling. Aging provides a particularly informative setting in which to examine this interface, because mitochondrial dysfunction and lysosomal decline co-emerge and reinforce one another during cellular aging. Current evidence suggests that aging does not simply increase or decrease MLCs, but instead remodels their dynamics, molecular composition, and functional output. Such remodeling may impair mitophagy, alter calcium and lipid coupling, amplify oxidative and inflammatory stress, and contribute to age-related disease phenotypes. In this review, we summarize the structural organization and regulatory logic of MLCs, examine their mechanistic roles in organelle homeostasis, and discuss how aging reshapes this interface in physiological and pathological contexts. We also highlight key methodological challenges and therapeutic opportunities for the field.
    Keywords:  Aging; Lysosome; Membrane contact sites; Mitochondria-lysosome contacts; Mitochondrial quality control; Organelle homeostasis
    DOI:  https://doi.org/10.1016/j.mad.2026.112191
  8. J Microsc. 2026 May 13.
      The secretory pathway is a central and evolutionarily conserved feature of eukaryotic cells, responsible for protein and lipid trafficking, membrane biogenesis, signalling, and cellular homeostasis. Its complexity, dynamic behaviour, and nanoscale organisation have made it a longstanding target of microscopy-driven investigation. In this review, we trace the parallel evolution of our understanding of the secretory pathway and imaging technologies, with a particular emphasis on plant cells, where unique architectural and functional features have challenged and enriched mechanistic models. We highlight the foundational role of electron microscopy (EM) in defining the ultrastructural organisation of secretory organelles and establishing directional models of intracellular transport, followed by the fluorescence microscopy revolution that enabled direct visualisation of cargo flux and organelle dynamics in living cells. The advent of super-resolution fluorescence techniques bridged the long-standing resolution gap between light microscopy and EM, revealing nanoscale compartmentalisation, membrane contact sites, and trafficking intermediates previously inaccessible in living cells. More recently, the integration of functional assays, optogenetics, and artificial intelligence-driven segmentation, denoising, and adaptive imaging now enables quantitative and high-throughput analysis of secretory architecture. Together, these advances have transformed the secretory pathway from a static morphological concept into a dynamic, increasingly mechanistically defined system. We conclude by discussing emerging integrative strategies, particularly correlative and AI-enhanced approaches that promise to unify ultrastructural precision with molecular specificity and temporal resolution in future studies of endomembrane organisation.
    Keywords:  Golgi bodies; artificial intelligence; endoplasmic reticulum; microscopy
    DOI:  https://doi.org/10.1111/jmi.70115
  9. Front Physiol. 2026 ;17 1826699
      The uncoupling of Mitochondria-ER Contact Sites (MERCS) represents a hallmark of metabolic dysfunction in obesity and type 2 diabetes. These are dynamic interfaces that play essential roles in coordinating ion signaling and lipid exchange to maintain cellular homeostasis. Persistent organelle stress in chronic disease impairs these pathways, driving systemic hormone resistance and metabolic failure. A paradigm shifts in glucagon-like peptide-1 receptor (GLP-1R) signaling from diffuse events to spatiotemporally organized signalosomes offer insightful mechanisms into these conditions. The localization of internalized GLP-1Rs at the Mitochondria-ER interface supports a contactomics framework for understanding bioenergetic restoration. Stabilizing inter-organellar connectivity represents a novel frontier for next-generation metabolic therapies.
    Keywords:  GLP-1 receptor (GLP-1R); GLP1 receptor agonist (GLP1-RAs); Mitochondria-ER Contact Sites (MERCS); metabolic dysfunction; signalosomes
    DOI:  https://doi.org/10.3389/fphys.2026.1826699
  10. Phytomedicine. 2026 May 04. pii: S0944-7113(26)00498-8. [Epub ahead of print]156 158264
       BACKGROUND: Myocardial ischemia-reperfusion injury (MIRI) constitutes a significant contributor to the increased incidence of post-ischemic heart failure. The primary mechanisms underlying MIRI involve oxidative stress and mitochondrial calcium overload in reperfused cardiomyocytes. Regulating the homeostasis of the mitochondrial-associated endoplasmic reticulum membranes (MAMs) to improve endoplasmic reticulum-mitochondrial communication is expected to treat MIRI, but there are currently no clear targeted drugs. The Shenfuyixin Granules (SFYX) exhibit capabilities in lowering reactive oxygen species levels, curtailing apoptosis, and improving mitochondrial performance in cardiomyocytes. However, its therapeutic role in MIRI remains unclear.
    AIM OF THE STUDY: This study aims to clarify the effect of SFYX on mitochondrial calcium overload after MIRI and elucidate its potential mechanism of action.
    METHODS: The rat MIRI model was established by short-time ligation of the left anterior descending coronary artery and reperfusion, and SXNI (3.275g/kg, 6.55g/kg, 13.1g/kg) was administered for treatment. Network pharmacology combined with molecular docking has revealed the specific molecular mechanism by which SFYX regulates mitochondrial calcium homeostasis in the myocardium. The improvement effect of SFYX on MIRI was evaluated by western blotting (WB), TUNEL staining, immunofluorescence staining, etc. A hypoxia/reoxygenation (H/R) model of myocardial cells was simultaneously established, MIRI was simulated in vitro, and the mechanism was verified using WB, fluorescent probes, mitochondrial function and other related tests.
    RESULTS: Network pharmacological analysis and molecular docking indicated that SFYX might improve MIRI by reducing mitochondrial calcium overload through the cGMP-PKG signaling pathway and calcium signaling pathway, and the key blood-entering components could stably bind to cGMP and PKG. In vivo experiments confirm that SFYX significantly attenuates myocardial injury associated with MIRI and alleviates levels of oxidative stress and apoptosis through the sGC/PKG pathway. In vitro experiments verify that SFYX regulates MAMs via the sGC/PKG signaling pathway, thereby stabilizing mitochondrial function, alleviating calcium overload and oxidative stress, and ultimately combating MIRI.
    CONCLUSION: This study suggests that SFYX prophylactic administration can alleviate mitochondrial calcium overload by targeting MAMs through the sGC/PKG signaling axis and has a preventive effect on MIRI. These findings indicate that SFYX may become a potential drug for preventing MIRI in the future.
    Keywords:  Mitochondria-associated endoplasmic reticulum membranes; Mitochondrial calcium overload; Myocardial ischemia reperfusion injury; Oxidative stress; Traditional chinese medicine
    DOI:  https://doi.org/10.1016/j.phymed.2026.158264
  11. Int Immunopharmacol. 2026 May 13. pii: S1567-5769(26)00685-5. [Epub ahead of print]182 116839
      Ferroptosis of cardiomyocytes is a key factor in myocardial ischemia-reperfusion injury (MIRI), but its regulatory mechanisms and intervention targets have not been fully clarified. Calcitonin gene-related peptide (CGRP) is a key regulatory factor released from peripheral vascular nerve endings, with powerful vasodilatory, positive chronotropic, and inotropic effects. In this study, the effects of CGRP on myocardial ischemia/reperfusion injury (I/R) and hypoxia/reoxygenation (H/R) were investigated in a rat model of left anterior descending coronary artery ligation and reperfusion. We found that the endogenous CGRP concentration in the serum of I/R rats was significantly decreased. While exogenous CGRP improved the viability of H/R cardiomyocytes in a concentration-dependent manner, inhibited the release of lactate dehydrogenase, down-regulated the expression of ferroptosis executive protein ACSL4, up-regulated the expression of GPX4, and reduced the accumulation of reactive oxygen species and lipid peroxide. Mechanistically, CGRP alleviates H/R-induced mitochondrial dynamics imbalance, improving mitochondrial morphology and membrane potential. In addition, CGRP inhibited abnormal expression of key proteins (IP3R, GRP75, and VDAC) at mitochondrial endoplasmic reticulum contact sites (MAMs) and reduced ferroptosis signaling. In vivo experiments demonstrated that nitroglycerin and cinnamaldehyde, a TRPA1 agonist, reduced myocardial infarction size by activating the TRPA1-CGRP pathway, while blocking the CGRP receptor could counteract this protective effect. In conclusion, our study demonstrates that CGRP mitigates myocardial ferroptosis through the regulation of mitochondrial dynamics and MAMs interactions. These findings establish CGRP as a promising therapeutic target and provide a solid theoretical foundation for combating myocardial I/R injury.
    Keywords:  CGRP; Ferroptosis; Ischemia and reperfusion; MAMs; Mitochondria dynamics
    DOI:  https://doi.org/10.1016/j.intimp.2026.116839
  12. Aging Cell. 2026 05;25(5): e70534
      Due to aging, the efficiency of kidney function begins to decrease. Dysfunction in mitochondria and their cristae is a hallmark of aging. Therefore, age-related decline in kidney function could be attributed to changes in mitochondrial ultrastructure, increased reactive oxygen species, and alterations in metabolism and lipid composition. We sought to understand how mitochondrial ultrastructure is altered over time in tubular kidney cells. A serial block face-scanning electron microscope and manual segmentation using the Amira software were employed to visualize murine kidney samples during the aging process at 3 months (young) and 2 years (old). We found that 2-year mitochondria are more fragmented with many uniquely shaped mitochondria observed across aging, concomitant with shifts in ROS, metabolomics, and lipid homeostasis. Furthermore, we demonstrate that the mitochondrial contact site and cristae organizing system (MICOS) complex is impaired in the kidney during aging. Disruption of the MICOS complex resulted in altered mitochondrial metabolic function and increased ROS levels. We found significant, detrimental structural changes in the mitochondria of aged kidney tubules, suggesting a potential mechanism underlying the increased frequency of kidney disease with aging. We hypothesize that disruption of the MICOS complex exacerbates mitochondrial dysfunction, creating a vicious cycle of mitochondrial degradation and oxidative stress, which impacts kidney health.
    Keywords:  3DEM; MICOS complex; kidney; metabolism; mitochondria
    DOI:  https://doi.org/10.1111/acel.70534