Journal
FEBS LETTERS
Volume 585, Issue 6, Pages 834-840Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.02.012
Keywords
c-Abl; Bcr-Abl; Mena; Abi-1; trans-Activation; Leukemic cell adhesion
Funding
- JSPS
- Grants-in-Aid for Scientific Research [22791382] Funding Source: KAKEN
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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. Structured summary of protein interactions: Abi1 physically interacts with c-Abl by pull down (View Interaction 1, 2) c-Abl physically interacts with Abi1 by anti bait coimmunoprecipitation (View Interaction 1, 2) c-Abl physically interacts with Abi1 by pull down (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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