Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation |
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Authors: | Smith Richard D Lupashin Vladimir V |
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Institution: | Department of Physiology and Biophysics, College of Medicine, University of Arkansas for Medical Sciences, Biomed 261-2, Slot 505, 200 South Cedar St., Little Rock, AR 72205, USA. |
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Abstract: | The Golgi apparatus is a central hub for both protein and lipid trafficking/sorting and is also a major site for glycosylation in the cell. This organelle employs a cohort of peripheral membrane proteins and protein complexes to keep its structural and functional organization. The conserved oligomeric Golgi (COG) complex is an evolutionary conserved peripheral membrane protein complex that is proposed to act as a retrograde vesicle tethering factor in intra-Golgi trafficking. The COG protein complex consists of eight subunits, distributed in two lobes, Lobe A (Cog1-4) and Lobe B (Cog5-8). Malfunctions in the COG complex have a significant impact on processes such as protein sorting, glycosylation, and Golgi integrity. A deletion of Lobe A COG subunits in yeasts causes severe growth defects while mutations in COG1, COG7, and COG8 in humans cause novel types of congenital disorders of glycosylation. These pathologies involve a change in structural Golgi phenotype and function. Recent results indicate that down-regulation of COG function results in the resident Golgi glycosyltransferases/glycosidases to be mislocalized or degraded. |
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Keywords: | CCD vesicles COG complex-dependent vesicles CDG congenital disorders of glycosylation CHO Chinese hamster ovary COG conserved oligomeric Golgi Con A concanavalin A fws four way stop GalNAcT2 N-acetylgalactosaminyltransferase-2 GalT galactosyltransferase GlcNAcT1 N-acetylglucosaminyltransferase I IEF isoelectric focusing LCA Lens culinaris agglutinin Ldl low-density lipoprotein PHA phytohemaglutinin PNA peanut agglutinin siRNA small interfering RNA WGA wheat germ agglutinin |
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