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Vol. 11, Issue 2, 613-626, February 2000
and
*Institute of Molecular Biology, Department of Chemistry,
University of Oregon, Eugene, Oregon 97403-1229; and
Mutations in the VPS (vacuolar protein sorting)
genes of Saccharomyces cerevisiae have been used to
define the trafficking steps that soluble vacuolar hydrolases take en
route from the late Golgi to the vacuole. The class D
VPS genes include VPS21, PEP12, and VPS45, which appear to encode
components of a membrane fusion complex involved in Golgi-to-endosome
transport. Vps21p is a member of the Rab family of small Ras-like
GTPases and shows strong homology to the mammalian Rab5 protein, which
is involved in endocytosis and the homotypic fusion of early endosomes.
Although Rab5 and Vps21p appear homologous at the sequence level, it
has not been clear if the functions of these two Rabs are similar. We
find that Vps21p is an endosomal protein that is involved in the
delivery of vacuolar and endocytosed proteins to the vacuole. Vacuolar
and endocytosed proteins accumulate in distinct transport intermediates
in cells that lack Vps21p function. Therefore, it appears that Vps21p
is involved in two trafficking steps into the prevacuolar/late
endosomal compartment.
Centre for Molecular and Cellular Biology, University of
Queensland, St. Lucia, Queensland 4072, Australia
Corresponding author. E-mail
address: stevens{at}molbio.uoregon.edu.
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