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Src-related protein-tyrosine kinases and their surface receptors
Biochemical and Biophsical Acta (1993)
  • Janice T. Telfer, University of Massachusetts - Amherst
  • C.E. Rudd
  • O. Janssen
  • K.V.S. Prasad
  • M. Raab
  • A. Dasilva
  • H. Yamamoto

The CD4-p56lck and CD8-p56lck complexes have served as a paradym for an expanding number of interactions between src-family members (p56lck, p59fyn, p56lyn, p55blk) and surface receptors. These interactions implicate src-related kinases in the regulation of a variety of intracellular events, from lymphokine production and cytotoxicity to the expression of specific nuclear binding proteins. Different molecular mechanisms appear to have evolved to facilitate the receptor-kinase interactions, including the use of N-terminal regions, SH2 regions and kinase domains. Variation exists in stoichiometry, affinity and the nature of signals generated by these complexes in cells. The CD4-p56lck complex differs from receptor-tyrosine kinases in a number of important ways, including mechanisms of kinase domain regulation and recruitment of substrates such as PI 3-kinase. Furthermore, they may have a special affinity for receptor-substrates such as the TcR zeta, MB1/B29 or CD5 receptors, and act to recruit other SH2-carrying proteins, such as ZAP-70 to the receptor complexes. Receptor-src kinase interactions represent the first step in a cascade of intracellular events within the protein-tyrosine kinase/phosphatase cascade.

Publication Date
Citation Information
Janice T. Telfer, C.E. Rudd, O. Janssen, K.V.S. Prasad, et al.. "Src-related protein-tyrosine kinases and their surface receptors" Biochemical and Biophsical Acta Vol. 1155 (1993)
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