Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases

  title={Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases},
  author={B. J. Mayer and H. Hirai and R. Sakai},
  journal={Current Biology},
  • B. J. Mayer, H. Hirai, R. Sakai
  • Published 1995
  • Biology, Medicine
  • Current Biology
  • BACKGROUND Non-receptor protein-tyrosine kinases often contain at least one Src homology 2 (SH2) domain, a protein module that binds with high affinity to tyrosine-phosphorylated peptides. [...] Key Method We use chimeric mutants with heterologous SH2 domains to demonstrate that the SH2 domain of the oncogenically transforming adaptor protein Crk, which is the SH2 domain predicted to bind with highest affinity (of those tested) to potential phosphorylation sites in p130, is best able to facilitate…Expand Abstract
    283 Citations
    Enhanced Phosphorylation of Src Family Kinase Substrates Containing SH2 Domain Binding Sites*
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    High-throughput phosphotyrosine profiling using SH2 domains.
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    Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.
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    Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase.
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    Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites.
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    Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.
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    Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
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    Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.
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