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© The Rockefeller University Press, 0021-9525/2002/4/405 $5.00
The Journal of Cell Biology, Volume 157, Number 3, April 29, 2002 405-415

Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function

¹ Department of Molecular Biology, Princeton University, Princeton, NJ 08544
² Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139
³ Departments of Pathology, Beth Israel Deaconess Medical Center, Boston, MA 02215
⁴ Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR 72205
⁵ Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63130

Address correspondence to Monty Krieger, Biology Department, Massachusetts Institute of Technololgy, Room 68-483, 77 Massachusetts Ave., Cambridge, MA 02139. Tel.: (617) 253-6793. Fax: (617) 258-5851. E-mail: krieger{at}mit.edu

Multiprotein complexes are key determinants of Golgi apparatus structure and its capacity for intracellular transport and glycoprotein modification. Three complexes that have previously been partially characterized include (a) the Golgi transport complex (GTC), identified in an in vitro membrane transport assay, (b) the ldlCp complex, identified in analyses of CHO cell mutants with defects in Golgi-associated glycosylation reactions, and (c) the mammalian Sec34 complex, identified by homology to yeast Sec34p, implicated in vesicular transport. We show that these three complexes are identical and rename them the conserved oligomeric Golgi (COG) complex. The COG complex comprises four previously characterized proteins (Cog1/ldlBp, Cog2/ldlCp, Cog3/Sec34, and Cog5/GTC-90), three homologues of yeast Sec34/35 complex subunits (Cog4, -6, and -8), and a previously unidentified Golgi-associated protein (Cog7). EM of ldlB and ldlC mutants established that COG is required for normal Golgi morphology. "Deep etch" EM of purified COG revealed an 37-nm-long structure comprised of two similarly sized globular domains connected by smaller extensions. Consideration of biochemical and genetic data for mammalian COG and its yeast homologue suggests a model for the subunit distribution within this complex, which plays critical roles in Golgi structure and function.

Key Words: GTC-90 protein; ldlB protein; ldlC protein; Sec34 protein; Sec35 protein

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