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J. Biol. Chem., Vol. 277, Issue 14, 12288-12293, April 5, 2002
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From the Yeast Vps10p is a receptor for transport of the
soluble vacuolar hydrolase carboxypeptidase Y to the lysosome-like
vacuole. Its functional equivalents in mammalian cells are the mannose 6-phosphate receptors that mediate sorting to lysosomes of mannose 6-phosphate-containing lysosomal proteins. A chimeric receptor was
constructed by substituting the cytoplasmic domain of
Mr 300,000 mannose 6-phosphate receptor with
the Vps10p cytoplasmic tail. Expression of the chimera in cells lacking
endogenous mannose 6-phosphate receptors resulted in a subcellular
receptor distribution and an efficiency in sorting of lysosomal enzymes
similar to that of the wild type Mr 300,000 mannose 6-phosphate receptor. Moreover, the cytoplasmic tail of the
Vps10p was found to interact with GGA1 and GGA2, two mammalian members
of a recently discovered family of clathrin-binding cytosolic proteins
that participate in trans-Golgi network-endosome
trafficking in both mammals and yeast. Our findings suggest a conserved
machinery for Golgi-endosome/vacuole sorting and may serve as a model
for future studies of yeast proteins.
The Yeast Vps10p Cytoplasmic Tail Mediates Lysosomal Sorting in
Mammalian Cells and Interacts with Human GGAs*
,¶
Universitätsklinikum Münster,
Institut für Physiologische Chemie und Pathobiochemie,
Waldeyerstrasse 15, Universität Münster, D-48149
Münster, Germany and the § Department of Medical
Biochemistry and Cell Biology, University of Aarhus,
DK-8000 Aarhus C, Denmark
*
This work was supported by the Danish Medical Research
Foundation, the Novo Nordic Foundation, and the Deutsche
Forschungsgemeinschaft.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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