Conserved oligomeric Golgi complex
The conserved oligomeric Golgi complex (COG) is a multiprotein complex found in the Golgi apparatus structure and involved in intracellular transport and glycoprotein modification.[1]
Earlier names for this complex were: the Golgi transport complex (GTC), the LDLC complex, which is involved in glycosylation reactions, and the SEC34 complex, which is involved in vesicular transport. These 3 complexes are identical and are termed the conserved oligomeric Golgi (COG) complex.[2][3]
Structure
The COG protein complex consists of eight subunits, in two lobes; Lobe A consists of COG1, COG2, COG3, COG4 and lobe B consists of COG5, COG6, COG7, COG8.[4]
Function
The conserved oligomeric Golgi complex plays important roles in maintaining structure and transport mechanisms within the Golgi apparatus.[1]
References
- ^ a b Ungar D, Oka T, Brittle EE, Vasile E, Lupashin VV, Chatterton JE, Heuser JE, Krieger M, Waters MG (Apr 2002). "Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function". J Cell Biol. 157 (3): 405–15. doi:10.1083/jcb.200202016. PMC 2173297. PMID 11980916.
- ^ "Entrez Gene: COG5 component of oligomeric golgi complex 5".
- ^ Ungar et al., 2002)
- ^ Smith RD, Lupashin VV (2008). "Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation". Carbohydr Res. 343 (12): 2024–31. doi:10.1016/j.carres.2008.01.034. PMC 2773262. PMID 18353293.
External links
- Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation. Smith & Lupashin. 2008
- The conserved oligomeric Golgi complex is required for fucosylation of N-glycans in Caenorhabditis elegans. 2012
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