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 have been termed the conserved oligomeric Golgi (COG) complex (Ungar et al., 2002).[supplied by OMIM][2]

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.[3]

Function

The conserved oligomeric Golgi complex plays important roles in maintaining the structure and transport mechanisms within the Golgi apparatus.[1]

Further reading

References

  1. 1 2 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.
  2. ↑ "Entrez Gene: COG5 component of oligomeric golgi complex 5".
  3. ↑ 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.


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