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Vol. 12, Issue 2, 475-485, February 2001
and
*Howard Hughes Medical Institute and Department of Molecular and
Cell Biology, University of California, 229 Stanley Hall, Berkeley,
California 94720-3206; A native immunoisolation procedure has been used to investigate the
role of clathrin-coated vesicles (CCVs) in the transport of vacuolar
proteins between the trans-Golgi network (TGN) and the
prevacuolar/endosome compartments in the yeast Saccharomyces cerevisiae. We find that Apl2p, one large subunit of the
adaptor protein-1 complex, and Vps10p, the carboxypeptidase Y
vacuolar protein receptor, are associated with clathrin molecules.
Vps10p packaging in CCVs is reduced in pep12Department of Biological
Chemistry, School of Medicine, University of California, Los Angeles,
California 90095; and Département de Biochimie
Médicale, Centre Médicale Universitaire, Université
de Genève, 1211 Geneva 4, Switzerland
and
vps34, two mutants that block Vps10p transport from
the TGN to the endosome. However, Vps10p sorting is independent of
Apl2p. Interestingly, a Vps10Ctp mutant lacking its
C-terminal cytoplasmic domain, the portion of the receptor responsible
for carboxypeptidase Y sorting, is also coimmunoprecipitated with
clathrin. Our results suggest that CCVs mediate Vps10p transport from
the TGN to the endosome independent of direct interactions between
Vps10p and clathrin coats. The Vps10p C-terminal domain appears to play
a principal role in retrieval of Vps10p from the prevacuolar
compartment rather than in sorting from the TGN.
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