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Protein phosphorylation and hormone action.

P Cohen1

  • 1Department of Biochemistry, The University, Dundee, U.K.

Proceedings of the Royal Society of London. Series B, Biological Sciences
|July 22, 1988
PubMed
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Cellular processes are controlled by protein kinases and phosphatases, which regulate protein phosphorylation. These enzymes form a network allowing extracellular signals to coordinate cellular functions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Cellular regulation relies on the balance between protein kinases and protein phosphatases.
  • Protein phosphorylation, affecting seryl, threonyl, and tyrosyl residues, modifies protein function.
  • Extracellular signals, mediated by second messengers, influence kinase and phosphatase activity.

Purpose of the Study:

  • To review recent work on the role of protein kinases and phosphatases in cellular processes.
  • To highlight the pleiotropic actions of a limited number of these enzymes.
  • To explain how these enzymes form a network for signal transduction and functional coordination.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of signaling pathways involving protein kinases and phosphatases.

Related Experiment Videos

  • Examination of the coordination of biochemical functions by extracellular signals.

    • Main Results:

    • A small number of protein kinases and protein phosphatases control diverse cellular processes.
    • These enzymes exhibit pleiotropic actions, affecting multiple targets.
    • An interlocking network of these enzymes integrates extracellular signals.

    Conclusions:

    • Protein kinases and phosphatases are central regulators of cellular activity.
    • Their coordinated action allows for complex cellular responses to external stimuli.
    • The pleiotropic nature of these enzymes underlies the diverse effects of hormones and signals.