TYROSINE PHOSPHORYLATION IS ESSENTIAL FOR MICROFILAMENT ASSEMBLY IN LYMPHOCYTES-B

被引：28

作者：

MELAMED, I ^{[1
]}

DOWNEY, GP ^{[1
]}

ROIFMAN, CM ^{[1
]}

机构：

[1] HOSP SICK CHILDREN,DEPT PEDIAT,DIV IMMUNOL & ALLERGY,TORONTO M5G 1X8,ONTARIO,CANADA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)90445-D

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 regulates the tyrosine kinase signal transduction pathway and it mediates a variety of morphological changes such as capping and membrane ruffling. The relationship between these two events is unclear. We show here that cross-linking the antigen receptor on human B lymphocytes, in addition to increasing tyrosine phosphorylation of specific substrates, induces the conversion of G-actin to F-actin. Preincubation of B lymphocytes with two different tyrphostins blocked anti-IgM-induced tyrosine phosphorylation and actin polymerization. The ability of the tyrphostins to block anti-IgM induced conversion of G-actin to F-actin indicates that a tyrosine kinase acts as an essential link between the B cell antigen receptor the early changes in cytoskeletal reorganization. © 1991.

引用

页码：1424 / 1429

页数：6

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