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J. Biol. Chem., Vol. 280, Issue 38, 32736-32745, September 23, 2005
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1
From the
Department of Biology and ¶Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, the Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan, the Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, ||Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Department of Pathology, and**The CBR Institute for Biomedical Research, Harvard Medical School, Boston, Massachusetts 02115
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 the structure and function of COG using Cog1 or Cog2 null Chinese hamster ovary cell mutants, fibroblasts from a patient with Cog7-deficient congenital disorders of glycosylation, and stable Cog5-deficient HeLa cells generated by RNA interference. Although 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 low density lipoprotein 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. This model of the subunit organization of COG is in excellent agreement with in vitro data presented in an accompanying paper (Ungar, D., Oka, T., Vasile, E., Krieger, M., and Hughson, F. M. (2005) J. Biol. Chem. 280, 32729–32735). 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.
Received for publication, May 20, 2005 , and in revised form, July 15, 2005.
Addendum—An independent analysis of the subunit connectivity map of the Saccharomyces cerevisiae COG complex (58) that is in good agreement with the models proposed here and in the accompanying paper (52) appeared after this paper had been reviewed.
* This work was supported by National Institutes of Health Grant GM59115 (to M. K.) and an American Heart Association grant-in-aid (to F. M. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.
1 To whom correspondence should be addressed. Tel.: 617-253-6793; Fax: 617-258-5851; E-mail: krieger{at}mit.edu.
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