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Vol. 14, Issue 4, 1610-1623, April 2003
and
Institute of Molecular Biology, University of Oregon,
Eugene, Oregon 97403-1229
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.
Corresponding author. E-mail address:
stevens{at}molbio.uoregon.edu.
Present addresses:
*Center for Molecular Medicine and Therapeutics,
Department of Medical Genetics, University of British Columbia,
Vancouver, BC Canada V5Z 4H4;
Department of Pharmacology,
University of Pennsylvania, Philadelphia, PA 19104.
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