Identification of B cell adaptor for PI3-kinase (BCAP) as an Abl interactor 1-regulated substrate of Abl kinases
Identification of B cell adaptor for PI3-kinase (BCAP) as an Abl interactor 1-regulated substrate of Abl kinases
复制标题
DOI:
10.1016/j.febslet.2005.04.052
复制
发表时间:
2005-06-06
期刊:
影响因子:
3.5
通讯作者:
Shishido, T
中科院分区:
文献类型:
--
作者:
Maruoka, M;Suzuki, J;Shishido, T
In previous work we showed that AN interactor 1 (Abi-1), by linking enzyme and substrate, promotes the phosphorylation of Mammalian Enabled (Mena) by c-Ab1. To determine whether this mechanism extends to other c-Ab1 substrates, we used the yeast two-hybrid system to search for proteins that interact with Abi-1. By screening a human leukocyte cDNA library, we identified BCAP (B-cell adaptor for phosphoinositide 3-kinase) as another Abi-1-interacting protein. Binding experiments revealed that the SH3 domain of Abi-1 and the C-terminal polyproline structure of BCAP are involved in interactions between the two. In cultured cells, Abi-1 promoted phosphorylation of BCAP not only by c-Ab1 but also by v-Ab1. The phosphorylation sites of BCAP by c-Ab1 were mapped to five tyrosine residues in the C-terminal region that are well conserved in mammals. These results show that Abi-1 promotes Ab1-mediated BCAP phosphorylation and suggest that Abi-1 in general coordinates kinase-substrate interactions. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.