Abstract
Protein phosphorylation represents a rapid and reversible post-translational regulation that enables a fast control of protein activation that play key roles in cell signaling. For instance, Mitogen Activated Protein Kinase (MAPK) pathways are activated upon sequential phosphorylations, resulting in phosphorylation of cyto-sol and nuclear targets. We focus here on MAPK ERK1/2 signaling that accounts for diverse cellular responses such as cell cycle progression, proliferation, differentiation , senescence, migration, formation of GAP junctions, cell adhesion, cell motil-ity, survival and apoptosis. We review the role of protein phosphorylation in MAPK ERK1/2 activation, in its regulation in time and space and how its dysregulation can lead to tumorigenesis.
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CITATION STYLE
Vargas-Ibarra, D., Velez-Vasquez, M., & Bermudez-Munoz, M. (2021). Regulation of MAPK ERK1/2 Signaling by Phosphorylation: Implications in Physiological and Pathological Contexts. In Post-Translational Modifications in Cellular Functions and Diseases. IntechOpen. https://doi.org/10.5772/intechopen.97061
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