ASSOCIATION OF ACTIVATED PHOSPHATIDYLINOSITOL 3-KINASE WITH P120(CBL) IN ANTIGEN RECEPTOR-LIGATED B-CELLS

被引：73

作者：

KIM, TJ

KIM, YT

PILLAI, S

机构：

[1] Cancer Center, Harvard Medical School, Massachusetts General Hospital, Boston, MA 02129, Charlestown Navy Yard

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1995年 / 270卷 / 46期

关键词：

D O I：

10.1074/jbc.270.46.27504

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：

A 120-kDa protein that is tyrosine-phosphorylated upon antigen receptor ligation in B lymphocytes has been identified as the product of the c-cbl protooncogene. Tyrosine phosphorylation of Cbl depends on the efficient association of membrane immunoglobulin heavy chains with the Ig alpha/beta heterodimer but is unimpaired in splenic B cells from the Xid mouse. Crosslinking of membrane IgM and membrane IgG, but not of CD40, leads to the tyrosine phosphorylation of Cbl. In receptor-ligated B lymphocytes, p120(cbl) associates with an 85-kDa protein that has been identified as the 85-kDa subunit of phosphatidylinositol 3-kinase.

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页码：27504 / 27509

页数：6

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