COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex

The conserved oligomeric Golgi (COG) complex is a peripheral membrane protein complex which orchestrates tethering of intra-Golgi vesicles. We found that COG1-4 (lobe A) and 5–8 (lobe B) protein assemblies are present as independent sub-complexes on cell membranes. Super-resolution microscopy demons...

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Bibliographic Details
Published in:Scientific reports 2016-07, Vol.6 (1), p.29139-29139, Article 29139
Main Authors: Willett, Rose, Blackburn, Jessica Bailey, Climer, Leslie, Pokrovskaya, Irina, Kudlyk, Tetyana, Wang, Wei, Lupashin, Vladimir
Format: Article
Language:English
Subjects:
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14/19
14/28
631/1647/328
631/80/313/1525
82/83
Antibodies
Humanities and Social Sciences
Membranes
multidisciplinary
Proteins
Science
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Summary:The conserved oligomeric Golgi (COG) complex is a peripheral membrane protein complex which orchestrates tethering of intra-Golgi vesicles. We found that COG1-4 (lobe A) and 5–8 (lobe B) protein assemblies are present as independent sub-complexes on cell membranes. Super-resolution microscopy demonstrates that COG sub-complexes are spatially separated on the Golgi with lobe A preferential localization on Golgi stacks and the presence of lobe B on vesicle-like structures, where it physically interacts with v-SNARE GS15. The localization and specific interaction of the COG sub-complexes with the components of vesicle tethering/fusion machinery suggests their different roles in the vesicle tethering cycle. We propose and test a novel model that employs association/disassociation of COG sub-complexes as a mechanism that directs vesicle tethering at Golgi membranes. We demonstrate that defective COG assembly or restriction of tethering complex disassembly by a covalent COG1-COG8 linkage is inhibitory to COG complex activity, supporting the model.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep29139