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The Protein Kinase Family

  • Kenneth A. Walsh
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)

Abstract

An ever-expanding list of protein kinases is now known to serve diverse physiological roles in cellular systems (Table I). By phosphorylating serine, threonine or tyrosine residues in target proteins, these enzymes transduce metabolic or hormonal signals with profound cellular consequences (Krebs & Beavo, 1979; Flockhart & Corbin, 1982; Nishizuka, 1984; Stull et al., 1985). Serine- or threonine-specific protein kinases were first found to exercise control of diverse metabolic processes. Tyrosine-specific protein kinases are now found both as domains of trans-membrane growth factor receptors and encoded by viral oncogenes (Sefton & Hunter, 1985). Thus, some protein kinases are integral membrane proteins that are directly involved in the transduction of extracellular signals for intracellular purposes. Others act as amplifiers of intracellular signals, as regulators of structural or enzymatic components of cells, and as the unregulated products of certain oncogenic lesions.

Keywords

Protein Kinase Myosin Light Chain Kinase Alignment Score Protein Kinase Family Gamma Subunit 
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

© Plenum Press, New York 1987

Authors and Affiliations

  • Kenneth A. Walsh
    • 1
  1. 1.Department of BiochemistrySJ-70 University of WashingtonSeattleUSA

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