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A more recent version of this article appeared on September 23, 2005
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M505558200v1
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Papers In Press, published online ahead of print July 28, 2005
J. Biol. Chem, 10.1074/jbc.M505558200
Submitted on May 20, 2005
Revised on July 15, 2005
Accepted on July 28, 2005

Genetic analysis of the subunit organization and function of the COG complex: Studies of Cog5 and Cog7 deficient mammalian cells

Toshihiko Oka, Eliza Vasile, Marsha Penman, Carl D. Novina, Derek M. Dykxhoorn, Daniel Ungar, Frederick M. Hughson, and Monty Krieger

Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139

Corresponding Author: krieger{at}mit.edu

The conserved oligomeric Golgi (COG) complex is an eight-subunit (Cog1-8) peripheral Golgi protein involved in Golgi-associated membrane trafficking and glycoconjugate synthesis. We have analyzed COG’s structure and function using Cog1- or Cog2-null CHO cell mutants, fibroblasts from a patient with Cog7 deficient congenital disorders of glycosylation and stable Cog5 deficient HeLa cells generated by RNA interference. While the dilation of some Golgi cisternae in Cog5 deficient cells resembled that observed in Cog1 or Cog2 deficient cells, their global glycosylation defects (less severe) and intracellular processing and function of LDL receptors (essentially normal) differed from Cog1 and Cog2 deficient cells. Immunoblotting, gel filtration and immunofluorescence microscopy analyses of the COG deficient cells and cell extracts indicated that 1) Cog2-4 and Cog5-7 form stable subcomplexes, 2) Cog1 mediates Golgi association of a Cog2-4 plus Cog8 subcomplex, 3) Cog8 associates stably with both Cog5-7 and Cog1-4 subcomplexes, and thus 4) Cog8 helps assemble the Cog1-4 and Cog5-7 subcomplexes into the complete COG complex. Only one or two of the seven Cog1- or Cog2-dependent Golgi membrane proteins called GEARs are also sensitive to Cog5 or Cog7 deficiency, indicating that the COG subunits play distinctive roles in controlling Golgi structure and function.


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