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Originally published In Press as doi:10.1074/jbc.M300267200 on March 3, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16844-16851, May 9, 2003
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The Adaptor Protein Fish Associates with Members of the ADAMs Family and Localizes to Podosomes of Src-transformed Cells*

Clare L. AbramDagger §, Darren F. Seals||, Ian Pass, Daniel Salinsky, Lisa Maurer**, Therese M. RothDagger Dagger , and Sara A. Courtneidge§§

From Dagger  SUGEN Inc., South San Francisco, California 94080 and  Van Andel Research Institute, Grand Rapids, Michigan 49503

Fish is a scaffolding protein and Src substrate. It contains an amino-terminal Phox homology (PX) domain and five Src homology 3 (SH3) domains, as well as multiple motifs for binding both SH2 and SH3 domain-containing proteins. We have determined that the PX domain of Fish binds 3-phosphorylated phosphatidylinositols (including phosphatidylinositol 3-phosphate and phosphatidylinositol 3,4-bisphosphate). Consistent with this, a fusion protein of green fluorescent protein and the Fish PX domain localized to punctate structures similar to endosomes in normal fibroblasts. However, the full-length Fish protein was largely cytoplasmic, suggesting that its PX domain may not be able to make intermolecular interactions in unstimulated cells. In Src-transformed cells, we observed a dramatic re-localization of some Fish molecules to actin-rich structures called podosomes; the PX domain was both necessary and sufficient to effect this translocation. We used a phage display screen with the fifth SH3 domain of Fish and isolated ADAM19 as a binding partner. Subsequent analyses in mammalian cells demonstrated that Fish interacts with several members of the ADAMs family, including ADAMs 12, 15, and 19. In Src-transformed cells, ADAM12 co-localized with Fish in podosomes. Because members of the ADAMs family have been implicated in growth factor processing, as well as cell adhesion and motility, Fish could be acting as an adaptor molecule that allows Src to impinge on these processes.

* The Fish research in S. A. C.'s laboratory was generously supported by the Van Andel Research Institute.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.

§ Contributed equally to this work.

|| Contributed equally to this work.

** Present address: Kenyon College, Gambier, OH 43022.

Dagger Dagger Present address: Program in Biomedical Sciences, University of Michigan, Ann Arbor, MI.

§§ To whom correspondence should be addressed: Van Andel Research Inst., 333 Bostwick N.E., Grand Rapids, MI 49503. Tel.: 616-234-5704; Fax: 616-234-5705; E-mail: sara.courtneidge@vai.org.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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