COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity.
Vesicular tethers and SNAREs are two key protein components that govern docking and fusion of intracellular membrane carriers in eukaryotic cells. The conserved oligomeric Golgi (COG) complex has been specifically implicated in the tethering of retrograde intra-Golgi vesicles. Using yeast two-hybrid and co-immunoprecipitation approaches, we show that the COG6 subunit of the COG complex is capable of interacting with a subset of Golgi SNAREs, namely STX5, STX6, GS27 and SNAP29. Interaction with SNAREs is accomplished via the universal SNARE-binding motif of COG6. Overexpression of COG6, or its depletion from cells, disrupts the integrity of the Golgi complex. Importantly, COG6 protein lacking the SNARE-binding domain is deficient in Golgi binding, and is not capable of inducing Golgi complex fragmentation when overexpressed. These results indicate that COG6-SNARE interactions are important for both COG6 localization and Golgi integrity.
Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR, USA.
Tetyana
T
Kudlyk
Rose
R
Willett
Irina D
ID
Pokrovskaya
Vladimir
V
Lupashin
D033942:Adaptor Proteins, Vesicular Transport / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D006056:Golgi Apparatus / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D009154:Mutation; D011485:Protein Binding; D034741:RNA, Small Interfering; D050600:SNARE Proteins / Q000235:genetics / Q000378:metabolism*; D022161:Transport Vesicles / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D033942:Adaptor Proteins, Vesicular Transport; C553748:COG6 protein, human; D034741:RNA, Small Interfering; D050600:SNARE Proteins