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Subunit architecture of the conserved oligomeric Golgi complex

Ungar, D., Oka, T., Vasile, E., Krieger, M. and Hughson, F.M. (2005) Subunit architecture of the conserved oligomeric Golgi complex. Journal of Biological Chemistry, 280 (38). pp. 32729-32735. ISSN 0021-9258

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Abstract

The conserved oligomeric Golgi (COG) complex is thought to function in intra-Golgi retrograde trafficking mediated by coat protein I vesicles, a pathway essential for the proper structure and function of the Golgi apparatus. Previous work suggested that COG might act as a tethering factor to mediate the initial attachment between coat protein I vesicles and Golgi membranes. Here, we present extensive in vitro co-translation and immunoprecipitation experiments leading to a new model for the overall architecture of the mammalian COG complex. The eight COG subunits (Cog1–8) are found to form two heterotrimeric subassemblies (Cog2/3/4 and Cog5/6/7) linked by a heterodimer composed of the remaining subunits (Cog1/8). This model is in excellent agreement with in vivo data presented in an accompanying paper (Oka, T., Vasile, E., Penman, M., Novina, C. D., Dykxhoorn, D. M., Ungar, D., Hughson, F. M., and Krieger, M. (2005) J. Biol. Chem. 280, 32736–32745).

Item Type: Article
Institution: The University of York
Academic Units: The University of York > Biology (York)
Depositing User: York RAE Import
Date Deposited: 07 May 2009 13:08
Last Modified: 07 May 2009 13:08
Published Version: http://dx.doi.org/10.1074/jbc.M504590200
Status: Published
Publisher: The American Society for Biochemistry and Molecular Biology
Identification Number: 10.1074/jbc.M504590200
URI: http://eprints.whiterose.ac.uk/id/eprint/6511

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