First Author | Pleiman CM | Year | 1994 |
Journal | Science | Volume | 263 |
Issue | 5153 | Pages | 1609-12 |
PubMed ID | 8128248 | Mgi Jnum | J:178287 |
Mgi Id | MGI:5297796 | Doi | 10.1126/science.8128248 |
Citation | Pleiman CM, et al. (1994) Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit. Science 263(5153):1609-12 |
abstractText | Engagement of antigen receptor complexes induces rapid activation of Src-family kinases and association with phosphatidylinositol-3' kinase (PI-3 kinase). Here it was found that the Src homology 3 (SH3) domain of Lyn and Fyn bound to a proline-rich region (residues 84 to 99) within the 85-kilodalton subunit (p85) of PI-3 kinase. The binding of SH3 to the purified kinase led to a five- to sevenfold increase in the specific activity of PI-3 kinase. Ligand-induced receptor stimulation activated PI-3 kinase, and this activation was blocked by a peptide containing residues 84 to 99 of p85. These data demonstrate a mechanism for PI-3 kinase activation and show that binding of SH3 domains to proline-rich target sequences can regulate enzymatic activity. |