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Originally published In Press as doi:10.1074/jbc.M909368199 on March 9, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16030-16036, May 26, 2000
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Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, Domains*

Mark T. BedfordDagger §, Adam Frankel||, Michael B. Yaffe**Dagger Dagger , Steven Clarke, Philip LederDagger , and Stéphane Richard§§¶¶

From the Dagger  Department of Genetics, Harvard Medical School, Howard Hughes Medical Institute, Boston, Massachusetts 02115, the  Molecular Biology Institute and Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095-1569, the ** Department of Surgery and Division of Signal Transduction, Beth Israel Deaconess Medical Center, Harvard Institute of Medicine, Boston, Massachusett 02115, and the §§ Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital and the Departments of Oncology, Medicine and Microbiology and Immunology, McGill University, Montreal, Quebec H3T 1E2, Canada

Src homology 3 (SH3) and WW domains are known to associate with proline-rich motifs within their respective ligands. Here we demonstrate that the proposed adapter protein for Src kinases, Sam68, is a ligand whose proline-rich motifs interact with the SH3 domains of p59fyn and phospholipase Cgamma -1 as well as with the WW domains of FBP30 and FBP21. These proline-rich motifs, in turn, are flanked by RG repeats that represent targets for the type I protein arginine N-methyltransferase. The asymmetrical dimethylation of arginine residues within these RG repeats dramatically reduces the binding of the SH3 domains of p59fyn and phospholipase Cgamma -1, but has no effect on their binding to the WW domain of FBP30. These results suggest that protein arginine methylation can selectively modulate certain protein-protein interactions and that mechanisms exist for the irreversible regulation of SH3 domain-mediated interactions.

* This work was supported in part by Medical Research Council of Canada Grant MT-13377 (to S. R.) and by National Institutes of Health Grant GM26020 (to S. 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.

§ Supported in part by Award 1440 from the Cancer Research Fund of the Damon Runyon-Walter Winchell Foundation.

|| Supported in part by National Institutes of Health Training Grant GM 07185.

Dagger Dagger Supported by National Institutes of Health Grant HL03601 and a Harvard Medical School Joint Research Initiative award.

¶¶ Scholar of the Medical Research Council. To whom correspondence should be addressed: Molecular Oncology Group, Lady Davis Inst., 3755 Côte Ste-Catherine Rd., Montreal, Quebec H3T 1E2, Canada. Tel.: 514-340-8260; Fax: 514-340-7576; E-mail: mcrd@musica.mcgill.ca.

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