Abstract
Extracellular signal-regulated kinases 1 and 2 (ERKs) are central regulators of many physiological and pathological processes. Their activity is regulated by phosphorylation on both tyrosine and threonine residues within their activation loops by MAPK / ERK kinases 1 and 2 (MEKs). Removal of phosphate from either the tyrosine, the threonine, or from both residues together can inactivate ERKs. Indeed members of the three groups of protein phosphatases, protein Ser / Thr phosphatase, protein Tyr phosphatase, and dual specificity phosphatases have been implicated in the inactivation of ERKs. In this review, we describe the various mechanisms involved in the inactivation of ERKs during different stages of mitogenic stimulation of quiescent cells.
Keywords: erk, mapk, mkp, protein tyr phosphatase, protein ser thr phosphatase
Current Genomics
Title: The Molecular Mechanism of MAPK / ERK Inactivation
Volume: 5 Issue: 4
Author(s): Zhong Yao and Rony Seger
Affiliation:
Keywords: erk, mapk, mkp, protein tyr phosphatase, protein ser thr phosphatase
Abstract: Extracellular signal-regulated kinases 1 and 2 (ERKs) are central regulators of many physiological and pathological processes. Their activity is regulated by phosphorylation on both tyrosine and threonine residues within their activation loops by MAPK / ERK kinases 1 and 2 (MEKs). Removal of phosphate from either the tyrosine, the threonine, or from both residues together can inactivate ERKs. Indeed members of the three groups of protein phosphatases, protein Ser / Thr phosphatase, protein Tyr phosphatase, and dual specificity phosphatases have been implicated in the inactivation of ERKs. In this review, we describe the various mechanisms involved in the inactivation of ERKs during different stages of mitogenic stimulation of quiescent cells.
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Cite this article as:
Yao Zhong and Seger Rony, The Molecular Mechanism of MAPK / ERK Inactivation, Current Genomics 2004; 5 (4) . https://dx.doi.org/10.2174/1389202043349309
DOI https://dx.doi.org/10.2174/1389202043349309 |
Print ISSN 1389-2029 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5488 |
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