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• W1575763405 abstract "COPI vesicles serve for transport of proteins and membrane lipids in the early secretory pathway. Their coat protein (coatomer) is a heptameric complex that is recruited to the Golgi by the small GTPase Arf1 . Although recruited en bloc , coatomer can be viewed as a stable assembly of an adaptin‐like tetrameric subcomplex ( CM4 ) and a trimeric ‘cage’ subcomplex ( CM3 ). Following recruitment, coatomer stimulates ArfGAP ‐dependent GTP hydrolysis on Arf1 . Here, we employed recombinant coatomer subcomplexes to study the role of coatomer components in the regulation of ArfGAP2 , an ArfGAP whose activity is strictly coatomer‐dependent. Within CM4 , we define a novel hydrophobic pocket for ArfGAP2 interaction on the appendage domain of γ 1 ‐COP . The CM4 subcomplex (but not CM3 ) is recruited to membranes through Arf1 and can subsequently recruit ArfGAP2 . Neither CM3 nor CM4 in itself is effective in stimulating ArfGAP2 activity, but stimulation is regained when both subcomplexes are present. Our findings point to a distinct role of each of the two coatomer subcomplexes in the regulation of ArfGAP2 ‐dependent GTP hydrolysis on Arf1 , where the CM4 subcomplex functions in GAP recruitment, while, similarly to the COPII system, the cage‐like CM3 subcomplex stimulates the catalytic reaction." @default.
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• W1575763405 date "2012-03-28" @default.
• W1575763405 modified "2023-09-27" @default.
• W1575763405 title "Distinct Role of Subcomplexes of the COPI Coat in the Regulation of ArfGAP2 Activity" @default.
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• W1575763405 doi "https://doi.org/10.1111/j.1600-0854.2012.01349.x" @default.
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