Regulation of the phospholipase C-γ2 pathway in B cells

被引：0
作者：
Kurosaki, T [1 ]
机构：
[1] Kansai Med Univ, Dept Mol Genet, Inst Liver Res, Moriguchi, Osaka 5708506, Japan
[2] RIKEN, Lab Lymphocyte Differentiat, Res Ctr Allergy & Immunol, Moriguchi, Osaka 5708506, Japan
来源：
GENOME SCIENCE: TOWARDS A NEW PARADIGM? | 2002年 / 1246卷
关键词：
BCR; BLNK; PTKs; PLC-gamma; 2; IP3; receptors;
D O I：
10.1016/S0531-5131(02)01150-0
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：
Gene-targeting experiments in DT40 chicken B cells highlighted the importance of the intracellular protein tyrosine kinases Syk and Btk in phospholipase C (PLC)-gamma2 activation. Until recently, the molecular mechanism underlying the double requirement for Syk and Btk in PLC-gamma2 activation remained unclear, but new data suggest that an adaptor molecule, named BLNK, after being phosphorylated by Syk, provides docking sites for Btk SH2 domain as well as PLC-gamma2 SH2 domains, thus bringing Btk into close proximity with PLC-gamma2. The activated Btk then phosphorylates PLC-gamma2, leading to its activation. Inositol 1,4,5-trisphosphate OPA generated by PLC-gamma2 activation, binds to IP3 receptors, which is essential for triggering a calcium release from the endoplasmic reticulum (ER) and subsequent entry of extracellular calcium. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码：51 / 54
页数：4
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