@article{87026,
  keywords = {Proteins, Protein Structure, Tertiary, Humans, Biological Transport, Models, Biological, Membrane Proteins, Protein Binding, Protein Biosynthesis, Dimerization, Carrier Proteins, Immunoblotting, Plasmids, Electrophoresis, Polyacrylamide Gel, Immunoprecipitation, Two-Hybrid System Techniques, Golgi Apparatus, Adaptor Proteins, Vesicular Transport, Chromatography, Gel, Chromatography, Ion Exchange},
  author = {Daniel Ungar and Toshihiko Oka and Eliza Vasile and Monty Krieger and Frederick Hughson},
  title = {Subunit architecture of the conserved oligomeric Golgi complex.},
  abstract = {<p>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).</p>
},
  year = {2005},
  journal = {J Biol Chem},
  volume = {280},
  pages = {32729-35},
  month = {09/2005},
  issn = {0021-9258},
  doi = {10.1074/jbc.M504590200},
  language = {eng},
}