Biology: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
- ↑ 1.0 1.1 "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. Apr 2002. doi:10.1083/jcb.200202016. PMID 11980916.
- ↑ "Entrez Gene: COG5 component of oligomeric golgi complex 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10466.
- ↑ Ungar et al., 2002)
- ↑ "Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation". Carbohydr Res 343 (12): 2024–31. 2008. doi:10.1016/j.carres.2008.01.034. 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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