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COG complexes form spatial landmarks for distinct SNARE complexes

Author

Listed:
  • 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)

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.

Suggested Citation

  • Rose Willett & Tetyana Kudlyk & Irina Pokrovskaya & Robert Schönherr & Daniel Ungar & Rainer Duden & Vladimir Lupashin, 2013. "COG complexes form spatial landmarks for distinct SNARE complexes," Nature Communications, Nature, vol. 4(1), pages 1-13, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2535
    DOI: 10.1038/ncomms2535
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    Cited by:

    1. Di-Ao Liu & Kai Tao & Bin Wu & Ziyan Yu & Malwina Szczepaniak & Matthew Rames & Changsong Yang & Tatyana Svitkina & Yueyao Zhu & Fengyuan Xu & Xiaolin Nan & Wei Guo, 2023. "A phosphoinositide switch mediates exocyst recruitment to multivesicular endosomes for exosome secretion," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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