{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Le Vasseur M"],"funding":["Howard Hughes Medical Institute","National Heart, Lung, and Blood Institute","National Institutes of Health","National Institute of General Medical Sciences","National Human Genome Research Institute"],"pagination":["e67624"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8154037"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10"],"pubmed_abstract":["Dysfunction of the mitochondrial electron transport chain (mETC) is a major cause of human mitochondrial diseases. To identify determinants of mETC function, we screened a genome-wide human CRISPRi library under oxidative metabolic conditions with selective inhibition of mitochondrial Complex III and identified ovarian carcinoma immunoreactive antigen (OCIA) domain-containing protein 1 (OCIAD1) as a Complex III assembly factor. We find that OCIAD1 is an inner mitochondrial membrane protein that forms a complex with supramolecular prohibitin assemblies. Our data indicate that OCIAD1 is required for maintenance of normal steady-state levels of Complex III and the proteolytic processing of the catalytic subunit cytochrome c1 (CYC1). In OCIAD1 depleted mitochondria, unprocessed CYC1 is hemylat"],"journal":["eLife"],"pubmed_title":["Genome-wide CRISPRi screening identifies OCIAD1 as a prohibitin client and regulatory determinant of mitochondrial Complex III assembly in human cells."],"pmcid":["PMC8154037"],"funding_grant_id":["K99HL133372","R01GM126081","K99GM130964","S100D018223","HHMI","R00HL133372","1RM1HG009490","R37GM097432"],"pubmed_authors":["Le Vasseur M","Yamada J","Friedman J","Phinney BS","Nunnari J","Jost M","Horlbeck MA","Weissman JS","Kampmann M","Xu J","Salemi MR"],"additional_accession":[]},"is_claimable":false,"name":"Genome-wide CRISPRi screening identifies OCIAD1 as a prohibitin client and regulatory determinant of mitochondrial Complex III assembly in human cells.","description":"Dysfunction of the mitochondrial electron transport chain (mETC) is a major cause of human mitochondrial diseases. To identify determinants of mETC function, we screened a genome-wide human CRISPRi library under oxidative metabolic conditions with selective inhibition of mitochondrial Complex III and identified ovarian carcinoma immunoreactive antigen (OCIA) domain-containing protein 1 (OCIAD1) as a Complex III assembly factor. We find that OCIAD1 is an inner mitochondrial membrane protein that forms a complex with supramolecular prohibitin assemblies. Our data indicate that OCIAD1 is required for maintenance of normal steady-state levels of Complex III and the proteolytic processing of the catalytic subunit cytochrome c1 (CYC1). In OCIAD1 depleted mitochondria, unprocessed CYC1 is hemylat","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2025-04-04T10:18:17.876Z","creation":"2025-04-04T10:18:17.876Z"},"accession":"S-EPMC8154037","cross_references":{"pubmed":["34034859"],"doi":["10.7554/eLife.67624"]}}