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

作者: Jonathan A. Cooper , Tony Hunter

DOI: 10.1007/978-3-642-69075-4_4

关键词:

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

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