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Published online December 17, 2007
doi:10.1083/jcb.200705145
The Journal of Cell Biology, Vol. 179, No. 6, 1179-1192
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Shestakova et al.
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Article

 Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability

Anna Shestakova, Elena Suvorova, Oleksandra Pavliv, Galimat Khaidakova, and Vladimir Lupashin

Department of Physiology and Biophysics, College of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 72205

Correspondence to Vladimir Lupashin: vvlupashin{at}uams.edu

Tethering factors mediate initial interaction of transport vesicles with target membranes. Soluble N-ethylmaleimide–sensitive fusion protein attachment protein receptors (SNAREs) enable consequent docking and membrane fusion. We demonstrate that the vesicle tether conserved oligomeric Golgi (COG) complex colocalizes and coimmunoprecipitates with intra-Golgi SNARE molecules. In yeast cells, the COG complex preferentially interacts with the SNARE complexes containing yeast Golgi target (t)-SNARE Sed5p. In mammalian cells, hCog4p and hCog6p interact with Syntaxin5a, the mammalian homologue of Sed5p. Moreover, fluorescence resonance energy transfer reveals an in vivo interaction between Syntaxin5a and the COG complex. Knockdown of the mammalian COG complex decreases Golgi SNARE mobility, produces an accumulation of free Syntaxin5, and decreases the steady-state levels of the intra-Golgi SNARE complex. Finally, overexpression of the hCog4p N-terminal Syntaxin5a-binding domain destabilizes intra-Golgi SNARE complexes, disrupting the Golgi. These data suggest that the COG complex orchestrates vesicular trafficking similarly in yeast and mammalian cells by binding to the t-SNARE Syntaxin5a/Sed5p and enhancing the stability of intra-Golgi SNARE complexes.

A. Shestakova's present address is Dept. of Biology, University of Utah, Salt Lake City, UT 84112.

E. Suvorova's present address is Dept. of Microbiology, Montana State University, Bozeman, Montana 59717.

Abbreviations used in this paper: AD, activation domain; BD, binding domain; COG, conserved oligomeric Golgi; FRET, fluorescence resonance energy transfer; GalNAcT2, N-acetylgalactosaminyltransferase-2; GARP, Golgi-associated retrograde protein; HOPS, homotypic fusion and vacuole protein sorting; IF, immunofluorescence; IP, immunoprecipitation; KD, knockdown; WB, western blotting.


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