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Originally published In Press as doi:10.1074/jbc.M204869200 on October 23, 2002

J. Biol. Chem., Vol. 277, Issue 52, 50996-51002, December 27, 2002
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Endocytosis of Epidermal Growth Factor Receptor Regulated by Grb2-mediated Recruitment of the Rab5 GTPase-activating Protein RN-tre*

Lenka MartinuDagger , Ademi Santiago-Walker§, Hongwei QiDagger , and Margaret M. ChouDagger ||

From the Departments of Dagger  Cell and Developmental Biology and § Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

The Grb2 adaptor protein is best known for its role in signaling to the small GTPase p21ras, mediated through its interaction with the SOS guanine nucleotide exchange factor. Here, we demonstrate that Grb2 also signals to Rab5, a small GTPase that plays a key role in early endocytic trafficking. Grb2 functions through association with RN-tre, a GTPase-activating protein for Rab5. Grb2 and RN-tre associate both in vitro and in vivo, with interaction mediated by both SH3 domains of Grb2 and extended proline-rich sequences in RN-tre. Association between Grb2 and RN-tre is constitutive and occurs independently of Eps8, a previously identified binding partner of RN-tre. Epidermal growth factor (EGF) stimulates recruitment of RN-tre to the EGF receptor (EGFR) in a Grb2-dependent manner. Grb2 and the EGFR are internalized and co-localized in endocytic vesicles in response to EGF. Overexpression of RN-tre blocks the internalization of both proteins, consistent with its function as a negative regulator of Rab5 and endocytosis. Strikingly, RN-tre does not block EGF-induced internalization of a Grb2 mutant deficient in RN-tre binding. These results 1) suggest that the ability of RN-tre to inhibit internalization of the EGFR requires Grb2-mediated binding to the receptor and 2) identify Grb2 as a critical regulator of Rab5 and EGFR endocytosis.

* This work was supported by National Institutes of Health Grant RO1-CA81415-01A1 (to M. M. C.)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.

Current address: GlaxoSmithKline, 709 Swedeland Rd., King of Prussia, PA 19406.

|| To whom correspondence should be addressed: Dept. of Cell and Developmental Biology, 421 Curie Blvd. BRBII Rm. 1011, Philadelphia, PA 19104. Tel.: 215-573-4126; Fax: 215-898-9871; E-mail: mmc@ mail.med.upenn.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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