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J. Biol. Chem., Vol. 278, Issue 24, 21805-21813, June 13, 2003
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A Cortactin-CD2-associated Protein (CD2AP) Complex Provides a Novel Link between Epidermal Growth Factor Receptor Endocytosis and the Actin Cytoskeleton*
From the
Cancer Research Program, ¶Diabetes and Obesity Research Program and ||Protein Analysis Facility, Garvan Institute of Medical Research, St. Vincent's Hospital, Sydney, New South Wales 2010 and **Australian Proteome Analysis Facility, Macquarie University, Sydney, New South Wales 2109, Australia
Growth factor regulation of the cortical actin cytoskeleton is fundamental to a wide variety of cellular processes. The cortical actin-associated protein, cortactin, regulates the formation of dynamic actin networks via the actin-related protein (Arp)2/3 complex and hence is a key mediator of such responses. In order to reveal novel roles for this versatile protein, we used a proteomics-based approach to isolate cortactin-interacting proteins. This identified several proteins, including CD2-associated protein (CD2AP), as targets for the cortactin Src homology 3 domain. Co-immunoprecipitation of CD2AP with cortactin occurred at endogenous expression levels, was transiently induced by epidermal growth factor (EGF) treatment, and required the cortactin Src homology 3 domain. The CD2AP-binding site for cortactin mapped to the second of three proline-rich regions. Because CD2AP is closely related to Cbl-interacting protein of 85 kDa (CIN85), which regulates growth factor receptor down-regulation via complex formation with Cbl and endophilin, we investigated whether the CD2AP-cortactin complex performs a similar function. EGF treatment of cells led to transient association of Cbl and the epidermal growth factor receptor (EGFR) with a constitutive CD2AP-endophilin complex. Cortactin was recruited into this complex with slightly delayed kinetics compared with Cbl and the EGFR. Immunofluorescence analysis revealed that the EGFR, CD2AP, and cortactin co-localized in regions of EGF-induced membrane ruffles. Therefore, by binding both CD2AP and the Arp2/3 complex, cortactin links receptor endocytosis to actin polymerization, which may facilitate the trafficking of internalized growth factor receptors.
Received for publication, November 8, 2002 , and in revised form, March 20, 2003.
* This work was supported by the Department of Defense Breast Cancer Research Program Grant DAMD17-00-1-0251, which is managed by the United States Army Medical Research and Materiel Command, and by the National Health and Medical Research Council of Australia, the National Breast Cancer Foundation, and the Cancer Council New South Wales. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Both authors contributed equally to this work.
To whom correspondence should be addressed. Tel.: 61-2-9295-8333; Fax: 61-2-9295-8321; E-mail: r.daly{at}garvan.org.au.
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