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Vol. 11, Issue 1, 305-323, January 2000
Institute of Molecular Biology, University of Oregon, Eugene,
Oregon 97403-1229
The late Golgi of the yeast Saccharomyces cerevisiae
receives membrane traffic from the secretory pathway as well as
retrograde traffic from post-Golgi compartments, but the machinery that
regulates these vesicle-docking and fusion events has not been
characterized. We have identified three components of a novel protein
complex that is required for protein sorting at the yeast late Golgi
compartment. Mutation of VPS52, VPS53, or
VPS54 results in the missorting of 70% of the vacuolar
hydrolase carboxypeptidase Y as well as the mislocalization of late
Golgi membrane proteins to the vacuole, whereas protein traffic through
the early part of the Golgi complex is unaffected. A
vps52/53/54 triple mutant strain is phenotypically indistinguishable from each of the single mutants, consistent with the
model that all three are required for a common step in membrane
transport. Native coimmunoprecipitation experiments indicate that
Vps52p, Vps53p, and Vps54p are associated in a 1:1:1 complex that
sediments as a single peak on sucrose velocity gradients. This complex,
which exists both in a soluble pool and as a peripheral component of a
membrane fraction, colocalizes with markers of the yeast late Golgi by
immunofluorescence microscopy. Together, the phenotypic and biochemical
data suggest that VPS52, VPS53, and
VPS54 are required for the retrograde transport of Golgi
membrane proteins from an endosomal/prevacuolar compartment. The
Vps52/53/54 complex joins a growing list of distinct multisubunit
complexes that regulate membrane-trafficking events.
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