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Papers In Press, published online ahead of print January 18, 2002
UKM Muenster, Institut für Physiologische Chemie und Pathobiochemie, Muenster 48149
Corresponding Author: rpohlma{at}uni-muenster.de
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 wildtype Mr 300,000 mannose-6-phosphate receptor. Moreover, the cytoplasmic tail of the Vps10p was found to interact with GGA1 and -2, two mammalian members of a recently discovered family of clathrin binding cytosolic proteins that participate in TGN-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.
J. Biol. Chem, 10.1074/jbc.M112295200
Submitted on December 21, 2001
Revised on January 18, 2002
Accepted on January 18, 2002
The yeast Vps10p cytoplasmic tail mediates lysosomal sorting in mammalian cells and interacts with human GGAs
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