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Originally published In Press as doi:10.1074/jbc.M206868200 on August 19, 2002

J. Biol. Chem., Vol. 277, Issue 43, 41094-41100, October 25, 2002
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The Tetraspan Protein Epithelial Membrane Protein-2 Interacts with beta 1 Integrins and Regulates Adhesion*

Madhuri WadehraDagger §, Ramaswamy Iyer||, Lee Goodglick||**, and Jonathan BraunDagger ||**Dagger Dagger

From the Dagger  Molecular Biology Institute,  The David Geffen School of Medicine at UCLA and Jonsson Comprehensive Cancer Center, and the || Department of Pathology and Laboratory, Los Angeles, California 90095

The growth arrest-specific-3 (GAS3)/PMP22 proteins are members of the four-transmembrane (tetraspan) superfamily. Although the function of these proteins is poorly understood, GAS3/PMP22 proteins have been implicated in the control of growth and progression of certain cancers. Epithelial membrane protein-2 (EMP2), a GAS3/PMP22 family member, was recently identified as a putative tumor suppressor gene. Here, we addressed the normal function of EMP2 by testing the prediction that it influences integrin-related cell functions. We observed that EMP2 associates with the beta 1 integrin subunit. Co-immunoprecipitation and immunodepletion experiments indicated that ~60% of beta 1 integrins and EMP2 can be isolated in common protein complexes. Whereas this association between EMP2 and beta 1 integrin may be direct or indirect, it has features of integrin heterodimer selectivity. Thus, by laser confocal microscopy, EMP2 colocalized with alpha 6beta 1 but not alpha 5beta 1 integrin. Increased expression of EMP2 also influenced the integrin heterodimer repertoire present on the plasma membrane. EMP2 specifically increased the surface expression of the alpha 6beta 1 integrin while decreasing that of the alpha 5beta 1 protein. Reciprocally, reduction in EMP2 expression using a specific ribozyme decreased surface expression of alpha 6beta 1 integrin. Accordingly, these EMP2-mediated changes resulted in a dramatic alteration in cellular adhesion to extracellular matrix proteins. This study demonstrates for the first time the interaction of a GAS3/PMP22 family member with an integrin protein and suggests that such interactions and their functional consequences are a physiologic role of GAS3/PMP22 proteins.

* This work was supported by grants from the Lymphoma Research Foundation of America, the Irving Granet-MCL Foundation, the Ruzic Medical Research Foundation, the Jonsson Comprehensive Cancer Center (National Institutes of Health (NIH) Grant AI-28697), and the John Lloyd Foundation.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.

§ Supported by NIH Tumor Immunology Training Grant Fellowship 5-T32-CA009120-27.

** These authors contributed equally to this work.

Dagger Dagger To whom correspondence should be addressed: The David Geffen School of Medicine at UCLA, Department of Pathology and Laboratory Medicine, CHS 13-222, 10833 Le Conte Ave., Los Angeles, CA 90095-1732. Tel.: 310-825-0650; Fax: 310-825-5674; E-mail: jbraun@mednet.ucla.edu.

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