| Literature DB >> 17101133 |
Noriko Hirao1, Seiichi Sato, Tetsuya Gotoh, Masahiro Maruoka, Jun Suzuki, Satoru Matsuda, Tomoyuki Shishido, Katsuko Tani.
Abstract
Abl interactor (Abi) was identified as an Abl tyrosine kinase-binding protein and subsequently shown to be a component of the macromolecular Abi/WAVE complex, which is a key regulator of Rac-dependent actin polymerization. Previous studies showed that Abi-1 promotes c-Abl-mediated phosphorylation of Mammalian Enabled (Mena) and WAVE2. In addition to Abi-1, mammals possess Abi-2 and NESH (Abi-3). In this study, we compared the three Abi proteins in terms of the promotion of c-Abl-mediated phosphorylation and the formation of Abi/WAVE complex. Although Abi-2, like Abi-1, promoted the c-Abl-mediated phosphorylation of Mena and WAVE2, NESH (Abi-3) had no such effect. This difference was likely due to their binding abilities as to c-Abl. Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex. Our results suggest that NESH (Abi-3), like Abi-1 and Abi-2, is a component of the Abi/WAVE complex, but likely plays a different role in the regulation of c-Abl.Entities:
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Year: 2006 PMID： 17101133 DOI： 10.1016/j.febslet.2006.10.065
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124