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).
Highlights
The correct sorting of proteins into different compartments is crucial for every cell
The Golgi apparatus plays a central role in the secretory pathway, serving as a hub from which transport vesicles carrying different cargos depart toward different destinations [2]
Within the Golgi apparatus, the glycosylation enzymes that carry out these reactions maintain a nonuniform distribution through a balancing of anterograde and retrograde movement [5, 6]
Summary
The correct sorting of proteins into different compartments is crucial for every cell. We present extensive in vitro co-translation and immunoprecipitation experiments leading to a new model for the overall architecture of the mammalian COG complex. Subunits of the yeast COG complex interact with at least five Golgi SNAREs (14 –16, 26, 27).
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