Abstract
The reversible covalent modification of proteins by the addition and removal of a phosphate group is an important theme in signal transduction in mammalian cells. There is a large superfamily of protein kinases that catalyse the addition of a phosphate group to hydroxyl residues on the side chains of the amino acids serine, threonine, or tyrosine. Similarly there is a large family of protein phosphatases that catalyze the removal of phosphate groups from phosphoserine, phosphothreonine, and phosphotyrosine residues. A dynamic interplay between protein kinases and protein phosphatases exists in vivo whereby the phosphorylation status of the target protein is determined by the opposing actions of these kinases and phosphatases.
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Jones, M.L., Poole, A.W. (2004). Protein Tyrosine Phosphatases. In: Gibbins, J.M., Mahaut-Smith, M.P. (eds) Platelets and Megakaryocytes. Methods in Molecular Biology™, vol 273. Humana Press. https://doi.org/10.1385/1-59259-783-1:169
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DOI: https://doi.org/10.1385/1-59259-783-1:169
Publisher Name: Humana Press
Print ISBN: 978-1-58829-011-3
Online ISBN: 978-1-59259-783-3
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