<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Willett R</submitter><funding>NIGMS NIH HHS</funding><pagination>e27888</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3948154</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>4(1)</volume><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</pubmed_abstract><journal>Cellular logistics</journal><pubmed_title>Multipronged interaction of the COG complex with intracellular membranes.</pubmed_title><pmcid>PMC3948154</pmcid><funding_grant_id>R01 GM083144</funding_grant_id><pubmed_authors>Pokrovskaya I</pubmed_authors><pubmed_authors>Lupashin V</pubmed_authors><pubmed_authors>Kudlyk T</pubmed_authors><pubmed_authors>Willett R</pubmed_authors></additional><is_claimable>false</is_claimable><name>Multipronged interaction of the COG complex with intracellular membranes.</name><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</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Jan</publication><modification>2025-05-29T19:21:31.297Z</modification><creation>2025-05-29T19:21:31.297Z</creation></dates><accession>S-EPMC3948154</accession><cross_references><pubmed>24649395</pubmed><doi>10.4161/cl.27888</doi></cross_references></HashMap>