bims-mecosi Biomed News
on Membrane contact sites
Issue of 2026–03–15
nine papers selected by
Verena Kohler, Umeå University



  1. J Exp Bot. 2026 Mar 09. pii: erag127. [Epub ahead of print]
      Endoplasmic reticulum-plasma membrane contact sites (ER-PM CS) are central hubs that coordinate lipid metabolism, membrane remodelling, calcium signalling and stress responses in plant cells. This review summarizes current knowledge on the molecular architecture and functions of ER-PM CS, with emphasis on the three tether families (synaptotagmins/SYTs, multiple-C2-domain and transmembrane region proteins/MCTPs, and VAMP-associated protein 27/VAP27 proteins) and the lipid-transfer proteins (SMP-domain proteins and oxysterol-binding protein-related/ORPs) described to date. SYTs and MCTPs use C2 domains to read PM phosphoinositides and Ca2+ signals to dynamically modulate tethering, while VAP27s scaffold multimeric complexes via MSP-FFAT interactions and link the ER to the cytoskeleton. Lipid transfer at ER-PM CS sustain the phosphatidylinositol (PI) cycle and prevents accumulation of cone-shaped lipids such as diacylglycerol (DAG) at the PM. In plants, SYT1/SYT3 form a module with diacylglycerol kinases (DGKs) to clear DAG from the PM and to channel DAG into metabolism. ORP family members function as PI/PS (and sterol) exchangers and integrate contact-site lipid exchange with signalling and autophagy. ER-PM CS also intersect with endocytosis, autophagosome biogenesis, plasmodesmata function and unfolded protein response signalling, underlining their multi-functional roles in cellular homeostasis and stress adaptation.
    Keywords:  Endoplasmic reticulum; Lipid metabolism; MCTPs; Membrane contact sites; Membrane tethering; ORPs; Phosphatidylinositol cycle; Plasma membrane; SYTs; VAP27 proteins
    DOI:  https://doi.org/10.1093/jxb/erag127
  2. Int J Mol Sci. 2026 Feb 24. pii: 2117. [Epub ahead of print]27(5):
      Mitochondria-endoplasmic reticulum contacts (MERCs) are physical structures formed between mitochondria and the endoplasmic reticulum (ER) through various tethering proteins, playing crucial roles in multiple physiological processes, including Ca2+ and lipid exchange between the ER and mitochondria, regulation of mitochondrial morphology and dynamics (fusion and fission), as well as the induction of autophagy and apoptosis. Mitofusin 2 (MFN2), a key mitochondrial fusion protein, has been identified as an essential structural component of MERCs. Our research demonstrates that 16:8 circadian intermittent fasting (CIF) leads to enhanced mitochondrial fusion. The upregulation of MFN2 reinforces MERC stability, thereby facilitating efficient Ca2+ transfer between the ER and mitochondria. This process sustains the activity of mitochondrial oxidative phosphorylation (OXPHOS) enzymes, elevates mitochondrial oxygen utilization efficiency, and ultimately augments ATP production. Consequently, these adaptations enhance cardiomyocyte tolerance to hypoxic conditions. This study elucidates a novel mechanism by which MERCs regulate cellular hypoxia resistance and proposes a potential therapeutic strategy for improving acute hypoxia tolerance through the modulation of Ca2+ transport at MERCs.
    Keywords:  MERC; calcium transport; cardiomyocyte; circadian intermittent fasting; hypoxia; mitofusin 2
    DOI:  https://doi.org/10.3390/ijms27052117
  3. Diabetologia. 2026 Mar 08.
       AIMS/HYPOTHESIS: Postprandial glucagon-like peptide-1 (GLP-1) secretion by enteroendocrine L cells of the gut plays an important role in glucose homeostasis, thus representing a therapeutic option of ever-growing significance for type 2 diabetes. However, the precise mechanisms linking nutrient sensing and GLP-1 secretion are incompletely understood. In this study, we focused on a potential new role for endoplasmic reticulum (ER)-mitochondria contact sites, called mitochondria-associated membranes (MAMs), in nutrient-induced GLP-1 secretion by L cells, as they are dynamically regulated by nutrients, they influence cellular calcium homeostasis crucial for hormone secretion, and their miscommunication has been implicated in alterations of glucose homeostasis in several tissues.
    METHODS: We combined biochemical and imaging approaches to investigate nutrient-induced GLP-1 secretion, and ER-mitochondria interaction and calcium exchange in the STC-1 cell line, ex vivo ileal mouse organoids, and/or in vivo in gut enteroendocrine cells from Glu-Venus mice, both in acute conditions and after diet-induced obesity and type 2 diabetes.
    RESULTS: We show here that ER-mitochondria interactions are dynamically induced by two GLP-1 secretagogues, glucose and deoxycholic acid (DCA), in STC-1 cells (1.8- and 2.1-fold, respectively), ileal mouse organoids (1.7- and 1.3-fold, respectively), and in vivo in colonic L cells of Glu-Venus mice (1.3- and 1.2-fold, respectively). In addition, glucose increased ER-mitochondria calcium exchange in STC-1 cells (1.2-fold). A paracrine action of secreted GLP-1 was also involved in the regulation of MAMs by glucose and DCA in STC-1 cells. Dynamic reinforcement of MAMs by glucose and DCA played a causal role in GLP-1 release, as both pharmacological and genetic disruption of organelle communication blocked L cell secretory response to the two stimuli in STC-1 cells. In agreement, depleting ER calcium levels or inhibiting mitochondrial calcium entry decreased glucose-induced GLP-1 secretion (-37.5% and -30.9%, respectively), whereas inducing ER or mitochondrial stress prevented it (-47.9% and -51.8%, respectively). Mechanistically, glucose induces ER-mitochondria communication through a sodium-glucose cotransporter 1-mediated electrogenic effect, whereas DCA acts through a Takeda G protein-coupled receptor 5 (TGR5)-cAMP-protein kinase A (PKA) pathway. Finally, we demonstrated in C57Bl/6J mice and in Glu-Venus mice that diet-induced obesity reinforced basal ER-mitochondria interactions in colonic L cells and blocked their ability to respond to oral glucose in terms of both GLP-1 secretion and MAM upregulation.
    CONCLUSIONS/INTERPRETATION: These results point to a new role for ER-mitochondria calcium coupling in glucose-induced GLP-1 secretion in L cells of the gut, which is impaired in obesity and type 2 diabetes, providing a novel target for the modulation of GLP-1 secretion. Therefore, these data reinforce the potential targeting of MAMs to improve glycaemic outcomes in metabolic diseases.
    Keywords:  Enteroendocrine cells; GLP-1; Glucose homeostasis; Mitochondria-associated membrane; Nutrient sensing; Obesity; Type 2 diabetes
    DOI:  https://doi.org/10.1007/s00125-026-06693-7
  4. J Cell Biol. 2026 May 04. pii: e202506039. [Epub ahead of print]225(5):
      Bridge-like lipid transfer proteins (LTPs) contain a repeating β-groove domain and long hydrophobic grooves that act as bridges at membrane contact sites (MCSs) to efficiently transfer lipids. Atg2 is one such bridge-like LTP essential for autophagosome formation, during which a newly synthesized isolation membrane (IM) emerges and expands through lipid supply. However, studies on Atg2-mediated lipid transfer are limited to in vitro studies due to the lack of a suitable probe for monitoring phospholipid dynamics in vivo. Here, we characterized the lipophilic dye octadecyl rhodamine B (R18), which internalizes and labels the endoplasmic reticulum (ER) in a manner that requires flippases and oxysterol-binding protein-related proteins. Using R18, we demonstrated phospholipid transfer from the ER to the IM during autophagy in vivo. Upon autophagy termination, our data suggested the reversible phospholipid flow from the IM to the ER in response to environmental changes. Our findings highlight the critical role of bridge-like LTPs in MCS-mediated phospholipid homeostasis.
    DOI:  https://doi.org/10.1083/jcb.202506039
  5. J Ethnopharmacol. 2026 Mar 06. pii: S0378-8741(26)00314-4. [Epub ahead of print]364 121463
       ETHNOPHARMACOLOGICAL RELEVANCE: Maintenance of Ca2+ homeostasis at endoplasmic reticulum-mitochondria contact sites (MAMs) is a critical determinant of amelioration of post-ischemic brain injury and repair. Harpagide is a bioactive compound isolated from traditional Chinese medicine Radix Scrophulariae that shows potent anti-ischemic injury by regulating calcium homeostasis between MAMs. Nevertheless, the exact molecular pathways by which harpagide exerts these actions and identification of its direct cellular targets remain unresolved.
    AIM OF THE STUDY: This study aims to elucidate the time-dependent therapeutic potential and molecular mechanism of harpagide in ischemic injury, with particular emphasis on Grp75 and calcium homeostasis at MAMs.
    METHODS: Mouse middle cerebral artery occlusion (MCAO6h,8h)and PC12 cell oxygen-glucose deprivation (OGD4h,6h,8h)models were established. Relative cerebral blood flow, 2,3,5-triphenyltetrazolium chloride (TTC) staining, and hematoxylin-eosin (H&E) staining were used to analyze the neuroprotective effects of harpagide in MCAO mice. In vitro assays included apoptosis, Ca2+ transfer from the ER to the mitochondria, ER-mitochondria contact site analysis, molecular docking, Western blotting, fluorescent immunocytochemistry, co-immunoprecipitation, RNA interference of Grp75, and LDH release measurement. These assays were used to evaluate the therapeutic effects and mechanisms of harpagide in cerebral ischemic injury.
    RESULTS: Harpagide reduced infarct volume and neurological deficits in MCAO6h and 8h mice and attenuated mitochondria-mediated apoptosis at 4 h, 6 h, and 8 h post- OGD in vitro. Harpagide regulated calcium homeostasis between MAMs following ischemic stroke via the IP3R1-Grp75-VDAC1 axis. Harpagide exhibited a time-dependent modulation of Grp75: a trend toward increased expression after 4 h of OGD observed along with enhancement of ER-to-mitochondria Ca2+ transfer and ER-mitochondria contact, but significantly downregulating Grp75 at 6 h and 8 h of OGD resulted in decreased Ca2+ overload and reduced contact. Co-immunoprecipitation revealed that harpagide transiently enhanced IP3R1-Grp75 binding, peaking at 4 h and declining by 6 h. Harpagide also attenuated OGD-induced Grp75-VDAC1 co-localization at 6 h. Further assays showed that the protective effect was associated with targeting of Grp75. Notably, the anti-OGD-mediated neuronal damage effect of harpagide was markedly inhibited by Grp75 knockdown, but reinforced by the overexpression of Grp75 at 4 h OGD.
    CONCLUSION: Harpagide reduced injury due to cerebral ischemia in vivo and in vitro. The mechanism may be through the modulation of Grp75 to regulate calcium homeostasis at MAMs and the phase-dependent, dichotomous function of Grp75 in cerebral ischemia.
    Keywords:  Ca(2+) homeostasis; Grp75; Harpagide; Ischemic stroke; MAMs
    DOI:  https://doi.org/10.1016/j.jep.2026.121463
  6. Int Dent J. 2026 Mar 05. pii: S0020-6539(26)00036-5. [Epub ahead of print]76(3): 109440
       INTRODUCTION AND AIMS: Human dental pulp stem cells (hDPSCs) play pivotal roles in the regeneration of pulp-dentin complex, yet their odontogenic differentiation is critically modulated by the inflammatory microenvironment. Protein kinase R-like endoplasmic reticulum kinase (PERK), a key regulator of endoplasmic reticulum stress, is highly enriched in mitochondria-associated endoplasmic reticulum membranes (MAMs) and exerts critical functions. However, its precise mechanisms in inflammatory regulation and cellular differentiation remain elusive. This study elucidates the PERK-centred regulatory mechanism in MAMs that governs inflammation-impaired odontogenic differentiation of hDPSCs, potentially involving IP3R-dependent calcium flux and dynamic protein interactions in MAMs.
    METHODS: Rat pulpitis models and in vitro lipopolysaccharide (LPS)-induced inflammatory models of hDPSCs were established to investigate the effects of PERK signalling in odontogenesis under inflammatory conditions. Lentivirus-mediated silencing of PERK was performed to evaluate its role in LPS-induced inflammation. Molecular mechanisms were analysed using RNA sequencing, immunofluorescence, and transmission electron microscopy analyses.
    RESULTS: LPS stimulation activated the PERK signalling pathway, significantly upregulating MAM-related molecules (IP3R, VDAC1, GRP75) and enhancing PERK/VDAC1 colocalization and the formation of endoplasmic reticulum-mitochondria coupling structures. PERK silencing effectively mitigated LPS-induced mitochondrial swelling, ER dilatation, and calcium influx dysregulation, while restoring alkaline phosphatase activity and odontogenic differentiation potential. Mechanistically, PERK suppressed hDPSC mineralization by modulating IP3R-mediated calcium signalling pathway in MAMs.
    CONCLUSION: This study demonstrates that LPS-induced inflammatory stress reprograms hDPSCs bioactivity via PERK-centric control of MAMs likely through quantitative enhancement, structure specialization, and functional potentiation. The underlying mechanisms may involve IP3R-mediated regulation of calcium ion influx and protein interactions within MAMs.
    Keywords:  Dental pulp; Endoplasmic reticulum stress; Mitochondria-associated membranes; Stem cells
    DOI:  https://doi.org/10.1016/j.identj.2026.109440
  7. Mol Neurobiol. 2026 Mar 11. pii: 493. [Epub ahead of print]63(1):
      Alzheimer's disease (AD) is a progressive neurodegenerative disorder marked by memory loss and cognitive decline, predominantly in the elderly (Alzheimer Disease International et al., 2015). Although amyloid-β peptide (Aβ), particularly in its oligomeric forms, has long been linked to AD pathogenesis (Chen 9:1205-1235 2017, Gaspar 2 394-400 2010), the mechanisms underlying its cellular toxicity remain unclear. Mitochondrial dysfunction is a consistent feature of AD (D'Alessandro 107:102713 2025), yet how Aβ drives these alterations is not fully understood. This review integrates recent evidence showing that Aβ accumulates on mitochondrial membranes (Cenini 21:3257-3272 2016, Manczak 23:5131-5146 2006, Sirk 5:1989-2003 2007), providing a mechanistic link between amyloid pathology and mitochondrial damage. We discuss how membrane-associated Aβ disrupts mitochondrial protein import by impairing the translocase of the outer membrane (TOM) complex (Cenini 21:3257-3272 2016, Sirk 5:1989-2003 2007) and interferes with voltage-dependent anion channel 1 (VDAC1) (Smilansky 52:30670-30683 2015), a key regulator of metabolite exchange and apoptosis. We further emphasize the role of mitochondria-associated membranes (MAMs) as critical sites for Aβ generation and transfer to mitochondria, where dysregulated cholesterol metabolism may amplify MAM activity and Aβ accumulation (Area-Gomez and Schon 38:90-96 2017, Monaghan 2:240287 2025). Altogether, we propose that mitochondrial membrane localization of Aβ is a central mechanism linking amyloid pathology to mitochondrial dysfunction in aging, highlighting new directions for mitochondria-targeted therapeutic strategies in AD.
    Keywords:  Amyloid-β; Cholesterol; Mitochondria; Mitochondria-associated membranes; Proteostasis; Translocase of outer membrane; Voltage-dependent anion channel
    DOI:  https://doi.org/10.1007/s12035-026-05786-z
  8. Cell Mol Biol Lett. 2026 Mar 07.
      
    Keywords:  Cancer; Diabetes; ER stress; Kidney disease; Mitochondria-associated membranes; Neurodegenerative disease; Therapeutics
    DOI:  https://doi.org/10.1186/s11658-026-00887-y
  9. Front Immunol. 2026 ;17 1775841
      Depression is a prevalent emotional disorder that significantly impacts global health. Its etiology is multifactorial, and current therapeutic options have notable limitations, underscoring the need to identify novel molecular targets and therapeutic strategies. Neuroinflammation is a key pathophysiological feature of depression, with microglia serving as innate immune cells in the central nervous system (CNS), playing a crucial role in neuroinflammation sensing and amplification. Mitochondria and lysosomes, which are responsible for energy metabolism and waste degradation, respectively, forms non-fusogenic interactions at mitochondrial-lysosomal contact sites (MLCs) in microglia, promoting physical contact and signal transduction, thereby modulating microglial metabolic states and inflammatory phenotypes. Disruption of MLCs can lead to reactive oxygen species (ROS) accumulation, enhanced pro-inflammatory cytokine production, and amplification of neuroinflammatory cascades, thereby accelerating the neuroinflammation-driven pathogenesis of depression. In this review, we focus on how microglial MLCs drive neuroinflammation and contribute to the pathophysiology of depression. First, this review explores how peripheral immune dysregulation, oxidative stress, and impaired autophagy initiate and sustain neuroinflammatory responses that exacerbate depressive behaviors. Then, this review elucidates how mitochondrial dysfunction and lysosomal pathology amplify inflammatory signaling and promote the progression of depressive neurobiology. It highlights microglial MLCs abnormalities as a crucial mechanistic hub, detailing how disrupted Ca²+ crosstalk, impaired autophagic flux, and redox imbalance reinforce depression-related neuroinflammatory circuits. Finally, it summarizes emerging therapeutic strategies aimed at restoring microglial MLCs-regulated pathways and proposes future research directions to facilitate the development of neuroinflammation-targeted antidepressant therapies.
    Keywords:  depression; lysosomes; mitochondria; mitochondria-lysosome contact sites; molecular pathways; neuroinflammation; therapeutic interventions
    DOI:  https://doi.org/10.3389/fimmu.2026.1775841