| Literature DB >> 12672821 |
Katsuko Tani1, Seiichi Sato, Taiko Sukezane, Hiroshi Kojima, Hidenori Hirose, Hidesaburo Hanafusa, Tomoyuki Shishido.
Abstract
Mammalian Enabled (Mena) is a mammalian homologue of Drosophila Enabled (Ena), which genetically interacts with Drosophila Abl tyrosine kinase. The signaling pathway involving c-Abl and Mena (Ena) is not fully understood. To find molecules that participate in the c-Abl/Mena pathway, we searched for Mena-binding proteins using a yeast two-hybrid system. We identified Abl interactor 1 (Abi-1), which is known to interact with c-Abl, as a binding protein for Mena. Binding analysis revealed that the Ena/Vasp homology 1 domain of Mena and the polyproline structure of Abi-1 are necessary for the interaction. The interaction between Mena and Abi-1 was also observed in a mammalian expression system. Importantly, Abi-1 dramatically promoted c-Abl-mediated tyrosine phosphorylation of Mena but not other substrates such as c-Cbl. Mutational analysis demonstrated that the phosphorylation site of Mena is Tyr-296. Our results suggest that Abi-1 regulates c-Abl-mediated phosphorylation of Mena by interacting with both proteins.Entities:
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Year: 2003 PMID: 12672821 DOI: 10.1074/jbc.M301447200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157