Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling.

DOI PDF 被引用文献9件
  • T Kurosaki
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • M Takata
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • Y Yamanashi
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • T Inazu
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • T Taniguchi
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • T Yamamoto
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.
  • H Yamamura
    Department of Cardiovascular Molecular Biology, Lederle Laboratories, Pearl River, New York 10965.

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<jats:p>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.</jats:p>

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