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J Biol Chem, Vol. 274, Issue 32, 22303-22312, August 6, 1999
From the Department of Biological Sciences, Wayne State University,
Detroit, Michigan 48202
Rab GTPases comprise a large family of monomeric
proteins that regulate a diverse number of membrane trafficking events,
including endocytosis. In this paper, we examine the subcellular
distribution and function of the GTPase Rab15. Our biochemical and
confocal immunofluorescence studies demonstrate that Rab15 associates
with the transferrin receptor, a marker for the early endocytic
pathway, but not with Rab7 or the cation-independent mannose
6-phosphate receptor, markers for late endosomal membranes.
Furthermore, Rab15 colocalizes with Rab4 and -5 on early/sorting
endosomes, as well as Rab11 on pericentriolar recycling endosomes.
Consistent with its localization to early endosomal membranes,
overexpression of the constitutively active mutant HArab15Q67L reduces
receptor-mediated and fluid phase endocytosis. Therefore, our
functional studies suggest that Rab15 may function as an inhibitory
GTPase in early endocytic trafficking.
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