Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

被引:202
作者
Bedford, MT
Frankel, A
Yaffe, MB
Clarke, S
Leder, P
Richard, S
机构
[1] Sir Mortimer B Davis Jewish Hosp, Lady Davis Inst Med Res, Terry Fox Mol Oncol Grp, Montreal, PQ H3T 1E2, Canada
[2] McGill Univ, Dept Oncol, Montreal, PQ H3T 1E2, Canada
[3] McGill Univ, Dept Med, Montreal, PQ H3T 1E2, Canada
[4] McGill Univ, Dept Microbiol & Immunol, Montreal, PQ H3T 1E2, Canada
[5] Harvard Univ, Inst Med, Beth Israel Deaconess Med Ctr, Dept Surg, Boston, MA 02115 USA
[6] Harvard Univ, Inst Med, Beth Israel Deaconess Med Ctr, Div Signal Transduct, Boston, MA 02115 USA
[7] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA
[8] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
[9] Harvard Univ, Sch Med, Howard Hughes Med Inst, Dept Genet, Boston, MA 02115 USA
关键词
D O I
10.1074/jbc.M909368199
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 p59(fyn) and phospholipase C gamma-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 p59(fyn) and phospholipase C gamma-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.
引用
收藏
页码:16030 / 16036
页数:7
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