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NESH (Abi‐3) is present in the Abi/WAVE complex but does not promote c‐Abl‐mediated phosphorylation

2006; Wiley; Volume: 580; Issue: 27 Linguagem: Inglês

10.1016/j.febslet.2006.10.065

1873-3468

Noriko Hirao, Seiichi Sato, Tetsuya Gotoh, Masahiro Maruoka, Jun Suzuki, Satoru Matsuda, Tomoyuki Shishido, Katsuko Tani,

Fungal Plant Pathogen Control

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.