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J. Biol. Chem., Vol. 280, Issue 30, 27613-27623, July 29, 2005

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Cog1p Plays a Central Role in the Organization of the Yeast Conserved Oligomeric Golgi Complex^*

Pierre Fotso, Yulia Koryakina, Oleksandra Pavliv, Arnold B. Tsiomenko, and Vladimir V. Lupashin

From the Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205

The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved peripheral membrane oligomeric protein complex that is involved in intra-Golgi protein trafficking. The COG complex is composed of eight subunits that are located in two lobes; Lobe A contains COG1–4, and Lobe B is composed of COG5–8. Both in vivo and in vitro protein-protein interaction techniques were applied to characterize interactions between individual COG subunits. In vitro assays revealed binary interactions between Cog2p and Cog3p, Cog2p and Cog4p, and Cog6p and Cog8p and a strong interaction between Cog5p and Cog7p. The two-hybrid assay confirmed these findings and revealed that Cog1p interacted with subunits from both lobes of the complex. Antibodies to COG subunits were utilized to determine the protein levels and membrane association of COG subunits in yeast cog1–8 mutants. As a result, we created a model of the protein-protein interactions within the yeast COG complex and proposed that Cog1p is a bridging subunit between the two COG lobes. In support of this hypothesis, we have demonstrated that Cog1p is required for the stable association between two COG subcomplexes.

Received for publication, April 27, 2005 , and in revised form, June 2, 2005.

^* This work was supported by National Science Foundation Grant MCB-0234822. 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 Figs. S1–S8.

To whom correspondence should be addressed: Dept. of Physiology and Biophysics, University of Arkansas for Medical Sciences, Biomed 261-2, Mail Slot 505, 200 South Cedar St., Little Rock, AR 72205. Tel.: 501-603-1170; Fax: 501-686-8167; E-mail: vvlupashin{at}uams.edu.

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