{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Willett R"],"funding":["NIGMS NIH HHS"],"pagination":["e27888"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3948154"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(1)"],"pubmed_abstract":["The conserved oligomeric Golgi complex is a peripheral membrane protein complex that orchestrates the tethering and fusion of intra-Golgi transport carriers with Golgi membranes. In this study we have investigated the membrane attachment of the COG complex and it's on/off dynamic on Golgi membranes. Several complimentary approaches including knock-sideways depletion, FRAP, and FLIP revealed that assembled COG complex is not diffusing from Golgi periphery in live HeLa cells. Moreover, COG subunits remained membrane-associated even in COG4 and COG7 depleted cells when Golgi architecture was severely affected. Overexpression of myc-tagged COG sub-complexes revealed that different membrane-associated COG partners including β-COP, p115 and SNARE STX5 preferentially bind to different COG assembl"],"journal":["Cellular logistics"],"pubmed_title":["Multipronged interaction of the COG complex with intracellular membranes."],"pmcid":["PMC3948154"],"funding_grant_id":["R01 GM083144"],"pubmed_authors":["Pokrovskaya I","Lupashin V","Kudlyk T","Willett R"],"additional_accession":[]},"is_claimable":false,"name":"Multipronged interaction of the COG complex with intracellular membranes.","description":"The conserved oligomeric Golgi complex is a peripheral membrane protein complex that orchestrates the tethering and fusion of intra-Golgi transport carriers with Golgi membranes. In this study we have investigated the membrane attachment of the COG complex and it's on/off dynamic on Golgi membranes. Several complimentary approaches including knock-sideways depletion, FRAP, and FLIP revealed that assembled COG complex is not diffusing from Golgi periphery in live HeLa cells. Moreover, COG subunits remained membrane-associated even in COG4 and COG7 depleted cells when Golgi architecture was severely affected. Overexpression of myc-tagged COG sub-complexes revealed that different membrane-associated COG partners including β-COP, p115 and SNARE STX5 preferentially bind to different COG assembl","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jan","modification":"2025-05-29T19:21:31.297Z","creation":"2025-05-29T19:21:31.297Z"},"accession":"S-EPMC3948154","cross_references":{"pubmed":["24649395"],"doi":["10.4161/cl.27888"]}}