Protein tyrosine kinases in the initiation of antigen receptor signaling

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Abstract

Intracellular responses to antigen receptor engagement involve the activation of protein tyrosine kinases and the tyrosine phosphorylation of cellular proteins, including components of the antigen receptor. Phosphorylation of two tyrosine residues within an 18 amino acid segment of the cytoplasmic domain of antigen receptor subunits, and the subsequent association of either the Syk or Zap protein tyrosine kinase, has recently been shown to be required for successful antigen receptor signal propagation. The recent finding that distinct primary human immunodeficiencies result from mutations in genes encoding two non-transmembrane protein tyrosine kinases underscores the importance of this class of enzyme in antigen receptor signal transduction.

References (54)

  • G.W. Chacko et al.

    Clustering of the platelet Fcγ receptor induces noncovalent association with the tyrosine kinase p72syk

    J Biol Chem

    (1994)
  • N.S.C. Van Oers et al.

    ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ξ in murine thymocytes and lymph node T cells

    Immunity

    (1994)
  • A.C. Chan et al.

    Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling

    J Immunol

    (1994)
  • C.L. Law et al.

    Molecular cloning of human syk

    J Biol Chem

    (1994)
  • N. Isakov et al.

    ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity

    J Exp Med

    (1995)
  • L. Shiue et al.

    Interaction of p72syk with the γ and β subunits of the high affinity receptor for immunoglobulin E, FcϵRI

    Mol Cell Biol

    (1995)
  • E. Arpaia et al.

    Defective T cell receptor signaling and CD8+ thymic selection in humans lacking Zap-70 kinase

    Cell

    (1994)
  • W. Kolanus et al.

    T cell activation by clustered tyrosine kinases

    Cell

    (1993)
  • M.R. Clark et al.

    Analysis of Igα-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Igα stimulation of Fyn activity

    EMBO J

    (1994)
  • D. Davidson et al.

    Unique catalytic properties dictate the enhanced function of p59fynT, the hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T cells

    Mol Cell Biol

    (1993)
  • L.M.L. Chow et al.

    Negative regulation of T-cell receptor signaling by tyrosine protein kinase p50csk

    Nature

    (1993)
  • A. DeFranco

    Structure and function of the B cell antigen receptor

    Annu Rev Cell Biol

    (1993)
  • Mustelin T: T cell receptor signaling: three families of tyrosine kinases and a phosphatase. Immunity 1:...
  • C.I.E. Smith et al.

    X-linked agammaglobulinemia and other immunoglobulin deficiencies

    Immunol Rev

    (1994)
  • E.A. Clark et al.

    How B and T cells talk to each other

    Nature

    (1994)
  • M. Reth

    Antigen receptor tail clue

    Nature

    (1992)
  • T. Pawson et al.

    SH2 and SH3 domains: from structure to function

    Cell

    (1992)
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