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Biochem Biophys Res Commun. 1991 May 15;176(3):1424-9.

Tyrosine phosphorylation is essential for microfilament assembly in B lymphocytes.

Author information

1
Department of Pediatrics, Hospital for Sick Children, Toronto, Ontario, Canada.

Abstract

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.

PMID:
2039521
DOI:
10.1016/0006-291x(91)90445-d
[Indexed for MEDLINE]

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