| First Author | Sato M | Year | 2011 |
| Journal | FEBS Lett | Volume | 585 |
| Issue | 6 | Pages | 834-40 |
| PubMed ID | 21320496 | Mgi Jnum | J:201300 |
| Mgi Id | MGI:5512945 | Doi | 10.1016/j.febslet.2011.02.012 |
| Citation | Sato M, et al. (2011) Identification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1. FEBS Lett 585(6):834-40 |
| abstractText | Abi-1 is an adaptor protein for Abelson kinase (c-Abl), and Abi-1 promotes the Abl-mediated phosphorylation of Mammalian Enabled (Mena) by binding both c-Abl and Mena. Here, we identified a new phosphorylation site (Y398) in the SH3 domain of Abi-1, and disruption of Y398, combined with the previously identified phosphorylation site Y213, significantly weakens the binding of Abi-1 to c-Abl. The SH3 domain of Abi-1 and the proline-rich domain of c-Abl are involved in this interaction. Abi-1 phosphorylation at both sites stimulates the phosphorylation of Mena through the activation of c-Abl kinase. The phosphorylation of Abi-1 also plays a role in enhancing the adhesion of Bcr-Abl-transformed leukemic cells. |
