{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chu Q"],"funding":["National Natural Science Foundation of China"],"pagination":["94-110"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9883271"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["30(1)"],"pubmed_abstract":["In metazoans the endoplasmic reticulum (ER) undergoes extensive remodeling during the cell cycle. The endosomal sorting complexes required for transport (ESCRT) protein CHMP7 coordinates ESCRT-III dependent nuclear envelope reformation during mitotic exit. However, potential roles of ER-associated CHMP7 at non-mitotic stages remain unclear. Here we discovered a new role of CHMP7 in mediating three-way ER and ER-mitochondrial membrane contact sites (MCSs). We showed that CHMP7 localizes to multiple cellular membranes including the ER, mitochondrial-associated membranes (MAMs) and the outer mitochondrial membrane (OMM) via its N-terminal membrane-binding domain. CHMP7 undergoes dynamic assembly at three-way ER junctions and ER-mitochondrial MCSs through hydrophobic interactions among α helix-1 and α helix-2 of the C-terminal CHMP-like domain, which was required for tethering different organelles in vivo. Furthermore, CHMP7 mediates the formation of three-way ER junctions in parallel with Atlastins (ATLs). Importantly, CHMP7 also regulates ER-mitochondrial interactions and its depletion affects mitochondrial division independently of ESCRT complex. Taken together, our results suggest a direct role of CHMP7 in the formation of the ER contacts in interphase."],"journal":["Cell death and differentiation"],"pubmed_title":["Oligomeric CHMP7 mediates three-way ER junctions and ER-mitochondria interactions."],"pmcid":["PMC9883271"],"funding_grant_id":["81901166"],"pubmed_authors":["Chu Q","Xiong J","Ji WK","Shi A","Zhou T","Du Y","Deng L","Wang J"],"additional_accession":[]},"is_claimable":false,"name":"Oligomeric CHMP7 mediates three-way ER junctions and ER-mitochondria interactions.","description":"In metazoans the endoplasmic reticulum (ER) undergoes extensive remodeling during the cell cycle. The endosomal sorting complexes required for transport (ESCRT) protein CHMP7 coordinates ESCRT-III dependent nuclear envelope reformation during mitotic exit. However, potential roles of ER-associated CHMP7 at non-mitotic stages remain unclear. Here we discovered a new role of CHMP7 in mediating three-way ER and ER-mitochondrial membrane contact sites (MCSs). We showed that CHMP7 localizes to multiple cellular membranes including the ER, mitochondrial-associated membranes (MAMs) and the outer mitochondrial membrane (OMM) via its N-terminal membrane-binding domain. CHMP7 undergoes dynamic assembly at three-way ER junctions and ER-mitochondrial MCSs through hydrophobic interactions among α helix-1 and α helix-2 of the C-terminal CHMP-like domain, which was required for tethering different organelles in vivo. Furthermore, CHMP7 mediates the formation of three-way ER junctions in parallel with Atlastins (ATLs). Importantly, CHMP7 also regulates ER-mitochondrial interactions and its depletion affects mitochondrial division independently of ESCRT complex. Taken together, our results suggest a direct role of CHMP7 in the formation of the ER contacts in interphase.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-28T02:08:12.766Z","creation":"2025-02-19T01:45:28.182Z"},"accession":"S-EPMC9883271","cross_references":{"pubmed":["35962186"],"doi":["10.1038/s41418-022-01048-2"]}}