FEBS Lett 1995,
PMID: 7589581
Takata, M; Kurosaki, T
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.
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Text Mining Data
Syk → Src-PTK: "
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
"
Syk → Src-PTK: "
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
"
BCR → Src-PTK: "
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
"
BCR → Src-PTK: "
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
"
Src-PTK → BCR: "
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
"
Src-PTK → BCR: "
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
"
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