BANK regulates BCR-induced calcium mobilization by promoting tyrosine phosphorylation of IP3 receptor

被引:149
作者
Yokoyama, K
Su, I
Tezuka, T
Yasuda, T
Mikoshiba, K
Tarakhovsky, A
Yamamoto, T [1 ]
机构
[1] Univ Tokyo, Inst Med Sci, Dept Oncol, Tokyo 1088639, Japan
[2] Univ Tokyo, Inst Med Sci, Dept Mol Neurobiol, Tokyo 1088639, Japan
[3] Rockefeller Univ, Lab Lymphocyte Signaling, New York, NY 10021 USA
关键词
B-cell antigen receptor; calcium mobilization; inositul 1,4,5-trisphosphate receptor; scaffold protein; tyrosine phosphorylation;
D O I
10.1093/emboj/21.1.83
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
B-cell activation mediated through the antigen receptor is dependent on activation of protein tyrosine kinases (PTKs) such as Lyn and Syk and subsequent phosphorylation of various signaling proteins. Here we report on the identification and characterization of the B-cell scaffold protein with ankyrin repeats (BANK), a novel substrate of tyrosine kinases. BANK is expressed in B cells and is tyrosine phosphorylated upon B-cell antigen receptor (BCR) stimulation, which is mediated predominantly by Syk. Overexpression of BANK in B cells leads to enhancement of BCR-induced calcium mobilization. We found that both Lyn and inositol 1,4,5-trisphosphate receptor (IP3R) associate with the distinct regions of BANK and that BANK promotes Lyn-mediated tyrosine phosphorylation of IP3R. Given that IP3R channel activity is up-regulated by its tyrosine phosphorylation, BANK appears to be a novel scaffold protein regulating BCR-induced calcium mobilization by connecting PTKs to IP3R. Because BANK expression is confined to functional BCR-expressing B cells, BANK-mediated calcium mobilization may be specific to foreign antigen-induced immune responses rather than to signaling required for B-cell development.
引用
收藏
页码:83 / 92
页数:10
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