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Originally published In Press as doi:10.1074/jbc.M000344200 on June 2, 2000

J. Biol. Chem., Vol. 275, Issue 35, 26754-26764, September 1, 2000
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Rab15 Differentially Regulates Early Endocytic Trafficking*

Patricia A. ZukDagger and Lisa A. Elferink§

From the Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202

Rab GTPases play an important regulatory role in early endocytosis. We recently demonstrated that epitope-tagged Rab15 (HArab15) co-localizes with Rab4, -5, and -11 on early endosomal membranes in CHO cells (Zuk, P. A., and Elferink, L. A. (1999) J. Biol. Chem. 274, 22303-22312). To characterize the role of Rab15 in endocytosis, we prepared functional mutants of HArab15 and examined their effects on early endocytic trafficking. Wild-type HArab15 and its constitutively active, GTP-bound mutant (Q67L) reduce fluid phase and receptor-mediated endocytosis without affecting the rate of recycling from early endosomal compartments. Inhibition of early endocytosis appears to be due to a reduction in the rate of homotypic early endosome fusion. Conversely, mutations that constitutively inactivate HArab15 stimulate early endocytosis and the homotypic fusion of early endosomes in vitro. Unlike active forms of HArab15, constitutively inactive HArab15 mutants also affect recycling from early endosomal compartments. Moreover, the two constitutively inactive mutants, GDP-bound HArab15-T22N and the non-nucleotide binding mutant HArab15-N121I, differentially regulate the transit of fluid phase and receptor-mediated endocytic tracers through early/sorting endosomes. Together, these data suggest that HArab15 may counteract the reported stimulatory effect of Rab5 on early endocytosis. Consistent with this, overexpression of constitutively active HArab15-Q67L attenuates Rab5-stimulated endocytosis, whereas Rab5-stimulated endocytosis is augmented in cells overexpressing a constitutively inactive HArab15 mutant defective in guanine nucleotide binding (N121I). Our data indicate that HArab15 differentially regulates distinct steps in membrane trafficking through early/sorting and pericentriolar recycling endosomes.

* This work was supported in part by National Science Foundation Grant IBN-9974517 (to L. A. E.).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.

Dagger Supported in part by a William Turner Jr. Memorial Scholarship. Present address: Division for Plastic and Reconstructive Surgery, Center for Health Sciences, University of California, Los Angeles, 650 Charles E. Young Dr. S., Los Angeles, CA 90095.

§ To whom correspondence should be addressed: Dept. of Biological Sciences, 5047 Gullen Mall, Wayne State University, Detroit, MI 48202. Tel.: 313-577-5149; Fax: 313-577-6891; E-mail: laelferi@sun.science. wayne.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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