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Tyrosine phosphorylation of the Wiskott‐Aldrich Syndrome protein by Lyn and Btk is regulated by CDC42
Author(s) -
Guinamard Rodolphe,
Aspenström Pontus,
Fougereau Michel,
Chavrier Philippe,
Guillemot Jean-Claude
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01016-3
Subject(s) - wiskott–aldrich syndrome protein , lyn , bruton's tyrosine kinase , tyrosine phosphorylation , phosphorylation , microbiology and biotechnology , cdc42 , tyrosine kinase , biology , proto oncogene tyrosine protein kinase src , tyrosine , wiskott–aldrich syndrome , receptor tyrosine kinase , rac1 , signal transduction , cancer research , gtpase , actin cytoskeleton , cytoskeleton , biochemistry , cell , gene
The Wiskott‐Aldrich syndrome (WAS) is a rare immunodeficiency disease affecting mainly platelets and lymphocytes. Here, we show that the WAS gene product, WASp, is tyrosine phosphorylated upon aggregation of the high affinity IgE receptor (FcϵRI) at the surface of RBL‐2H3 rat tumor mast cells. Lyn and the Bruton's tyrosine kinase (Btk), two protein tyrosine kinases involved in FcϵRI‐signaling phosphorylate WASp and interact with WASp in vivo. Interestingly, expression of a GTPase defective mutant form of CDC42, that interacts with WASp, is accompanied by a substantial increase in WASp tyrosine phosphorylation. This study suggests that activated CDC42 recruits WASp to the plasma membrane where it becomes phosphorylated by Lyn and Btk. We conclude that WASp represents a connection between protein tyrosine kinase signaling pathways and CDC42 function in cytoskeleton and cell growth regulation in hematopoietic cells.