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The catalytic activity of Src‐family tyrosine kinase is required for B cell antigen receptor signaling
Author(s) -
Minoru Takata,
Tomohiro Kurosaki
Publication year - 1995
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 - 10.1016/0014-5793(95)01160-g
Subject(s) - lyn , proto oncogene tyrosine protein kinase src , tyrosine protein kinase csk , syk , sh2 domain , tyrosine kinase , cancer research , tyrosine phosphorylation , microbiology and biotechnology , b cell receptor , chemistry , receptor tyrosine kinase , phosphorylation , sh3 domain , signal transduction , biology , b cell , immunology , antibody
The Src family protein‐tyrosine kinases (PTKs) are known to be important for B cell antigen receptor (BCR) signaling. To study the mechanism of action of Src‐PTK in BCR signaling, kinase deficient‐ and Src homology 2 (SH2)‐mutants of Src‐PTK were transfected into Lyn‐deficient B cells and analyzed. Kinase activity of Src‐PTK was essential for tyrosine phosphorylation of Syk and calcium mobilization upon receptor ligation, whereas these events were not affected by the mutation of SH2 domain. Receptor‐mediated tyrosine phosphorylation of Lyn was still observed in Syk‐deficient B cells. These results demonstrate that the BCR‐induced phosphorylation of Src‐PTK is independent of Syk and that the kinase activity of Src‐PTK is critical for BCR signaling.