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Retroviruses 2 pp 125-161 | Cite as

Regulation of Cell Growth and Transformation by Tyrosine-Specific Protein Kinases: The Search for Important Cellular Substrate Proteins

  • Jonathan A. Cooper
  • Tony Hunter
Chapter
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 107)

Abstract

It is now well established that post-translational modification of vertebrate cell proteins can occur by phosphorylation at serine, threonine, and tyrosine. Many serine- and threonine-speciflc protein kinases and their substrates have been extensively characterized, and in several instances protein phosphorylation has been shown to play an important role in the regulation of cell metabolism through alteration of the properties of specific enzymes. Historically, evidence that modulation of protein function led to a significant change in metabolism often predated the discovery that the protein in question was a phosphoprotein and the isolation of the regulatory protein kinase. For example, increased glycogenolysis in liver slices, under conditions of adrenaline or glucagon treatment, was correlated with activation of the enzyme glycogen phosphorylase. The active form of glycogen phosphorylase was subsequently found to be a phosphoprotein, and the protein kinase responsible, phosphorylase kinase, was characterized (Krebs and Fischer 1956). The regulation of phosphorylase kinase itself by phosphorylation has since been elucidated in great detail (Cohen 1978).

Keywords

Tyrosine Phosphorylation Tyrosine Protein Kinase Murine Leukemia Virus Rous Sarcoma Virus Phosphoglycerate Mutase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1983

Authors and Affiliations

  • Jonathan A. Cooper
    • 1
  • Tony Hunter
    • 1
  1. 1.Molecular Biology and Virology LaboratoryThe Salk InstituteSan DiegoUSA

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