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Vol. 10, Issue 4, 875-890, April 1999
Division of Biological Sciences, University of Missouri, Columbia,
Missouri 65211
Resident membrane proteins of the trans-Golgi network (TGN) of
Saccharomyces cerevisiae are selectively retrieved from
a prevacuolar/late endosomal compartment. Proper cycling of the
carboxypeptidase Y receptor Vps10p between the TGN and
prevacuolar compartment depends on Vps35p, a hydrophilic peripheral
membrane protein. In this study we use a temperature-sensitive
vps35 allele to show that loss of Vps35p function
rapidly leads to mislocalization of A-ALP, a model TGN membrane
protein, to the vacuole. Vps35p is required for the prevacuolar
compartment-to-TGN transport of both A-ALP and Vps10p. This was
demonstrated by phenotypic analysis of vps35 mutant
strains expressing A-ALP mutants lacking either the retrieval or static
retention signals and by an assay for prevacuolar compartment-to-TGN
transport. A novel vps35 allele was identified that was
defective for retrieval of A-ALP but functional for retrieval of
Vps10p. Moreover, several other vps35 alleles were
identified with the opposite characteristics: they were defective for
Vps10p retrieval but near normal for A-ALP localization. These data
suggest a model in which distinct structural features within Vps35p are
required for associating with the cytosolic domains of each cargo
protein during the retrieval process.
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