BLNK required for coupling Syk to PLCγ2 and Rac1-JNK in B cells

被引：302

作者：

Ishiai, M

Kurosaki, M

Pappu, R

Okawa, K

Ronko, I

Fu, C

Shibata, M

Iwamatsu, A

Chan, AC

Kurosaki, T ^{[1
]}

机构：

[1] Kansai Med Univ, Inst Liver Res, Dept Mol Genet, Moriguchi, Osaka 5708506, Japan

[2] Washington Univ, Sch Med, Howard Hughes Med Inst, Dept Internal Med,Ctr Immunol,Div Rheumatol, St Louis, MO 63110 USA

[3] Washington Univ, Sch Med, Howard Hughes Med Inst, Dept Pathol,Div Rheumatol,Ctr Immunol, St Louis, MO 63110 USA

[4] Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 2360004, Japan

[5] Ina Lab, Med Biol Labs, Nagano 3960002, Japan

来源：

IMMUNITY | 1999年 / 10卷 / 01期

关键词：

D O I：

10.1016/S1074-7613(00)80012-6

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Signaling through the B cell receptor (BCR) is essential for B cell function and development. Despite the key role of Syk in BCR signaling, little is known about the mechanism by which Syk transmits downstream effecters. BLNK (B cell LiNKer protein), a substrate for Syk, is now shown to be essential in activating phospholipase C (PLC)gamma 2 and JNK. The BCR-induced PLC gamma S activation, but not the JNK activation, was restored by introduction of PLC gamma 2 membrane-associated form into BLNK-deficient B cells. As JNK activation requires both Rad and PLC gamma 2, our results suggest that BLNK regulates the Rac1-JNK pathway, in addition to modulating PLC gamma 2 localization.

引用

页码：117 / 125

页数：9

共 49 条

[1] SHIP modulates immune receptor responses by regulating membrane association of Btk [J].