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Diversity and Regulation of cAMP-Dependent Protein Kinases

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Molecular and Cellular Endocrinology of the Testis

Part of the book series: Ernst Schering Research Foundation Workshop ((SCHERING FOUND,volume 1))

Abstract

Reversible protein phosphorylation is a key regulatory mechanism in eukaryotic cells. Protein phosphorylation was first demonstrated to regulate the activity of glycogen phosphorylase in response to glucagon (Fischer and Krebs 1955; Sutherland and Wosilait 1955). A heat-stable factor mediating the effect of glucagon on the phosphorylation status of glycogen phosphorylase was next identified as 3’,5’-cyclic adenosine monophosphate (cAMP; Sutherland and Rall 1958), and the concept of cAMP as an intracellular second messenger to a wide range of hormones, neurotransmitters, and other signaling substances was developed (Robinson et al. 1971). The target for cAMP was purified and identified as a cAMP-regulated protein kinase (Walsh et al. 1968), termed cAMP-dependent protein kinase (cAK; EC 2.7.1.37).

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Authors
  1. K. Taskén
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  2. B. S. Skålhegg
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  3. K. A. Taskén
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  4. R. Solberg
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  5. F. O. Levy
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  6. T. Lea
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  7. T. Jahnsen
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  8. V. Hansson
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G. Verhoeven U.-F. Habenicht

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© 1994 Springer-Verlag Berlin Heidelberg

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Taskén, K. et al. (1994). Diversity and Regulation of cAMP-Dependent Protein Kinases. In: Verhoeven, G., Habenicht, UF. (eds) Molecular and Cellular Endocrinology of the Testis. Ernst Schering Research Foundation Workshop, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-22189-1_9

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  • DOI: https://doi.org/10.1007/978-3-662-22189-1_9

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-22191-4

  • Online ISBN: 978-3-662-22189-1

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