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Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p.

Multisubunit tethering complexes may contribute to the specificity of membrane fusion events by linking transport vesicles to their target membrane in an initial recognition event that promotes SNARE assembly. However, the interactions that link tethering factors to the other components of the vesicle fusion machinery are still largely unknown. We have previously identified three subunits of a Golgi-localized complex (the Vps52/53/54 complex) that is required for retrograde transport to the late Golgi. This complex interacts with a Rab and a SNARE protein found at the late Golgi and is related to two other multisubunit tethering complexes: the COG complex and the exocyst. Here we show that the Vps52/53/54 complex has an additional subunit, Vps51p. All four members of this tetrameric GARP (Golgi-associated retrograde protein) complex are required for two distinct retrograde transport pathways, from both early and late endosomes, back to the TGN. vps51 mutants exhibit a distinct phenotype suggestive of a regulatory role. Indeed, we find that Vps51p mediates the interaction between Vps52/53/54 and the t-SNARE Tlg1p. The binding of this small, coiled-coil protein to the conserved N-terminal domain of the t-SNARE therefore provides a crucial link between components of the tethering and the fusion machinery.

Pubmed ID: 12686613


  • Conibear E
  • Cleck JN
  • Stevens TH


Molecular biology of the cell

Publication Data

April 10, 2003

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM32448

Mesh Terms

  • Biological Transport, Active
  • Carrier Proteins
  • Cloning, Molecular
  • Endosomes
  • Golgi Apparatus
  • Macromolecular Substances
  • Membrane Fusion
  • Membrane Proteins
  • Models, Biological
  • Mutation
  • Recombinant Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Two-Hybrid System Techniques
  • Vesicular Transport Proteins