DUAL ROLE OF THE TYROSINE ACTIVATION MOTIF OF THE IG-ALPHA PROTEIN DURING SIGNAL-TRANSDUCTION VIA THE B-CELL ANTIGEN RECEPTOR

被引：157

作者：

FLASWINKEL, H ^{[1
]}

RETH, M ^{[1
]}

机构：

[1] MAX PLANCK INST IMMUNOBIOL, D-79108 FREIBURG, GERMANY

来源：

EMBO JOURNAL | 1994年 / 13卷 / 01期

关键词：

B CELLS; IMMUNOGLOBULINS; PROTEIN TYROSINE; KINASES; RECEPTORS;

D O I：

10.1002/j.1460-2075.1994.tb06237.x

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：

The B cell antigen receptor (BCR) is a multimeric protein complex consisting of the ligand binding immunoglobulin molecule and the Ig-alpha/beta heterodimer that mediates intracellular signalling by coupling the receptor to protein tyrosine kinases (PTKs). Transfection of the Ig-alpha deficient myeloma cell line J558L mu m with expression vectors coding for mutated Ig-alpha allowed us to test the function of the tyrosines in the cytoplasmic region of Ig-alpha in the context of the BCR. Furthermore we expressed Ig-alpha mutations as chimeric CD8-Ig-alpha molecules on K46 B lymphoma cells and tested their signalling capacity in terms of PTK activation and release of calcium. We show here that the conserved tyrosine residues in the cytoplasmic portion of Ig-cr have a dual role. First, they are required for efficient activation of PTKs during signal induction and second, one of them is subject to phosphorylation by activated src-related PTKs. Phosphorylation on tyrosine in the cytoplasmic portion of Ig-alpha is discussed as a possible mechanism to couple the BCR to SH2 domain-carrying molecules.

引用

页码：83 / 89

页数：7

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