{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nguyen TT"],"funding":["Howard Hughes Medical Institute","National Institutes of Health"],"pagination":["e84279"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9725753"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["Mitochondria are dynamic organelles that undergo cycles of fission and fusion at a unified platform defined by endoplasmic reticulum (ER)-mitochondria membrane contact sites (MCSs). These MCSs or nodes co-localize fission and fusion machinery. We set out to identify how ER-associated mitochondrial nodes can regulate both fission and fusion machinery assembly. We have used a promiscuous biotin ligase linked to the fusion machinery, Mfn1, and proteomics to identify an ER membrane protein, ABHD16A, as a major regulator of node formation. In the absence of ABHD16A, fission and fusion machineries fail to recruit to ER-associated mitochondrial nodes, and fission and fusion rates are significantly reduced. ABHD16A contains an acyltransferase motif and an α/β hydrolase domain, and point mutations in critical residues of these regions fail to rescue the formation of ER-associated mitochondrial hot spots. These data suggest a mechanism whereby ABHD16A functions by altering phospholipid composition at ER-mitochondria MCSs. Our data present the first example of an ER membrane protein that regulates the recruitment of both fission and fusion machineries to mitochondria."],"journal":["eLife"],"pubmed_title":["An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion."],"pmcid":["PMC9725753"],"funding_grant_id":["T32 Training Grants GM008759 and GM142607"],"pubmed_authors":["Nguyen TT","Voeltz GK"],"additional_accession":[]},"is_claimable":false,"name":"An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion.","description":"Mitochondria are dynamic organelles that undergo cycles of fission and fusion at a unified platform defined by endoplasmic reticulum (ER)-mitochondria membrane contact sites (MCSs). These MCSs or nodes co-localize fission and fusion machinery. We set out to identify how ER-associated mitochondrial nodes can regulate both fission and fusion machinery assembly. We have used a promiscuous biotin ligase linked to the fusion machinery, Mfn1, and proteomics to identify an ER membrane protein, ABHD16A, as a major regulator of node formation. In the absence of ABHD16A, fission and fusion machineries fail to recruit to ER-associated mitochondrial nodes, and fission and fusion rates are significantly reduced. ABHD16A contains an acyltransferase motif and an α/β hydrolase domain, and point mutations in critical residues of these regions fail to rescue the formation of ER-associated mitochondrial hot spots. These data suggest a mechanism whereby ABHD16A functions by altering phospholipid composition at ER-mitochondria MCSs. Our data present the first example of an ER membrane protein that regulates the recruitment of both fission and fusion machineries to mitochondria.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2025-04-22T00:38:45.832Z","creation":"2025-04-05T19:35:37.81Z"},"accession":"S-EPMC9725753","cross_references":{"pubmed":["36448541"],"doi":["10.7554/eLife.84279"]}}