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Membrane detachment is not essential for COG complex function
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DOI：10.1091/mbc.E17-11-0694.png)
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Abstract
En 中文
The conserved oligomeric Golgi (COG) complex is a vesicle tether of the complexes associated with tethering containing helical rods family, which functions on the cytoplasmic side of Golgi. It is currently unknown whether COG function, or function of any multisubunit vesicular tether, depends on cycling between the membrane and cytosol. Therefore, we permanently anchored key subunits of COG subcomplexes (COG4, COG7, and COG8) to Golgi membranes using transmembrane protein TMEM115 (TMEM-COG). All TMEM-COG subunits tested were Golgi localized, integrated into the COG complex, and stabilized membrane association of endogenous subunits. Interestingly, TMEM-COG4 and TMEM-COG7 equally rescued COG function in organization of Golgi markers, glycosylation, and abundance of COG-sensitive proteins. In contrast, TMEM-COG8 was not as effective, indicating that N-terminal attachment of COG8 interfered with overall COG structure and function, and none of the TMEM-COG subunits rescued the abnormal Golgi architecture caused by COG knockout. Collectively, these data indicate that both subcomplexes of the COG complex can perform most of COG function when permanently attached to membranes and that the cytosolic pool of COG is not completely essential to COG function.
Keywords:
OLIGOMERIC GOLGI-COMPLEX
TETHERING COMPLEX
VESICLE DOCKING
PROTEIN COMPLEX
CATHEPSIN-D
IN-VIVO
GLYCOSYLATION
TRAFFICKING
COPI
TRANSPORT
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