COG complexes form spatial landmarks for distinct SNARE complexes

Rose Willett, Tetyana Kudlyk, Irina Pokrovskaya, Robert Schönherr, Daniel Ungar, Rainer Duden and Vladimir Lupashin ()
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Rose Willett: UAMS
Tetyana Kudlyk: UAMS
Irina Pokrovskaya: UAMS
Robert Schönherr: Institute of Biology, Center of Structural and Cell Biology in Medicine, University of Lübeck
Daniel Ungar: University of York
Rainer Duden: Institute of Biology, Center of Structural and Cell Biology in Medicine, University of Lübeck
Vladimir Lupashin: UAMS

Nature Communications, 2013, vol. 4, issue 1, 1-13

Abstract: Abstract Vesicular tethers and SNAREs (soluble N-ethylmalemide-sensitive fusion attachment protein receptors) are two key protein components of the intracellular membrane-trafficking machinery. The conserved oligomeric Golgi (COG) complex has been implicated in the tethering of retrograde intra-Golgi vesicles. Here, using yeast two-hybrid and co-immunoprecipitation approaches, we show that three COG subunits, namely COG4, 6 and 8, are capable of interacting with defined Golgi SNAREs, namely STX5, STX6, STX16, GS27 and SNAP29. Comparative analysis of COG8-STX16 and COG4-STX5 interactions by a COG-based mitochondrial relocalization assay reveals that the COG8 and COG4 proteins initiate the formation of two different tethering platforms that can facilitate the redirection of two populations of Golgi transport intermediates to the mitochondrial vicinity. Our results uncover a role for COG sub-complexes in defining the specificity of vesicular sorting within the Golgi.

Date: 2013
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DOI: 10.1038/ncomms2535

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