PMID:7513017

Citation	Kurosaki, T, Takata, M, Yamanashi, Y, Inazu, T, Taniguchi, T, Yamamoto, T and Yamamura, H (1994) Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling. J. Exp. Med. 179:1725-9
Abstract	Signaling through the B cell antigen receptor (BCR) results in rapid increases in tyrosine phosphorylation on a number of proteins. The BCR associates with two classes of tyrosine kinase: Src-family kinase (Src-protein-tyrosine kinase [PTK]; Lyn, Fyn, Blk, or Lck) and Syk kinase. We have investigated the interaction between the Src-PTK and the Syk kinase in the BCR signaling. In contrast to wild-type B cells, BCR-mediated tyrosine phosphorylation of Syk and activation of its in vitro kinase activity were profoundly reduced in lyn-negative cells. The requirement of the Src-PTK to induce tyrosine phosphorylation and activation of Syk was also demonstrated by cotransfection of syk and src-PTK cDNAs into COS cells. These results suggest that the Src-PTK associated with BCR phosphorylates the tyrosine residue(s) of Syk upon receptor stimulation, enhancing the activity of Syk.
Links	PubMed PMC2191497
Keywords	Animals; Cell Line; Enzyme Precursors/genetics; Enzyme Precursors/metabolism; Gene Expression Regulation; Intracellular Signaling Peptides and Proteins; Phosphorylation; Protein-Tyrosine Kinases/genetics; Protein-Tyrosine Kinases/metabolism; Proto-Oncogene Proteins pp60(c-src); Receptors, Antigen, B-Cell/metabolism; Signal Transduction; Transfection
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
MOUSE:KSYK		GO:0016310: phosphorylation	ECO:0000314:		P		Figure 1-Lyn dependent phosphorylation increases autophosphorylation activity of Syk through BCR stimulation	complete CACAO 6530

References

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