Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Serine/Threonine-Protein Phosphatase 2A

  • Veerle Janssens
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101865

Synonyms

Historical Background

Since Krebs and Fischer (1956) discovered that the activity of an enzyme (glycogen phosphorylase) can be regulated by a reversible phosphorylation, much attention has been paid to the enzymes catalyzing these covalent modifications: the protein kinases and protein phosphatases. As opposed to protein kinases, it has taken much more time to understand the action of protein phosphatases, mainly because of their complex molecular structure and broad substrate specificities. Nevertheless, protein phosphatases are equally important in controlling biochemical pathways, adding reversibility and sensitivity to these processes.

While the first kinase (phosphorylase kinase) was isolated soon after the discovery of the concept of reversible protein phosphorylation, the biochemical isolation of the first phosphataseneeded about 20 more years: ethanol denaturation (accidently...

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References

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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of Cellular and Molecular Medicine, Laboratory of Protein Phosphorylation and ProteomicsUniversity of Leuven (KU LEUVEN)LeuvenBelgium