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PMID: 11782428 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

BANK regulates BCR-induced calcium mobilization by promoting tyrosine phosphorylation of IP(3) receptor.

The EMBO journal ·Vol. 21 ·No. 1-2 ·2002-01-15 ·Pages 83-92

Yokoyama K, Su Ih IH, Tezuka T, Yasuda T, Mikoshiba K, Tarakhovsky A, Yamamoto T

Abstract

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. Overexpres sion 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 (IP(3)R) associate with the distinct regions of BANK and that BANK promotes Lyn-mediated tyrosine phosphorylation of IP(3)R. Given that IP(3)R 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 IP(3)R. 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.

MeSH Terms
Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Ankyrin Repeat B-Lymphocytes/immunology,metabolism Calcium Channels/metabolism Calcium Signaling/physiology Carrier Proteins/genetics,metabolism Humans Inositol 1,4,5-Trisphosphate Receptors Lymphocyte Activation Macromolecular Substances Membrane Proteins/genetics,metabolism Mice Mice, Knockout Mice, SCID Molecular Sequence Data Phosphorylation Receptors, Antigen, B-Cell/metabolism Receptors, Cytoplasmic and Nuclear/metabolism Sequence Homology, Amino Acid Tyrosine/metabolism src-Family Kinases/metabolism
Chemicals
Adaptor Proteins, Signal Transducing BANK1 protein, human Calcium Channels Carrier Proteins ITPR1 protein, human Inositol 1,4,5-Trisphosphate Receptors Macromolecular Substances Membrane Proteins Receptors, Antigen, B-Cell Receptors, Cytoplasmic and Nuclear Tyrosine lyn protein-tyrosine kinase src-Family Kinases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Yokoyama Kazumasa
Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
Su Ih I-hsin
Tezuka Tohru
Yasuda Tomoharu
Mikoshiba Katsuhiko
Tarakhovsky Alexander
Yamamoto Tadashi
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/21.1.83
Published
2002-01-15
Pages
83-92
Language
English
Region
England
NLM ID
8208664
PMCID
PMC125810
Subset
IM
Databases
GENBANK
AB063170
External Links
PubMed source DOI: 10.1093/emboj/21.1.83 PMC Full Text View journal details
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