Abstract
The phosphorylation of proteins at tyrosine residues is implicated in numerous cellular processes such as signal transduction, neoplastic transformation and the mitotic cycle. These processes are regulated by the activities of both protein-tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). PTPs represent a highly diversified and rapidly expanding family of enzymes (Fischer et al., 1991, Walton and Dixon, 1993). Indeed, since the identification of PTP1B six years ago (Tonks et al., 1988), more than 40 PTPs, excluding species homologies, have been identified. This is in striking contrast to the relatively small number of serine/threonine phosphatases identified over the past forty years. As with protein tyrosine kinases (PTK), there are two classes of PTPs: transmembrane (receptor-type) and intracellular enzymes. Most transmembrane PTPs have two conserved tandem intracellular catalytic domains with diversified receptor-like extracellular sequences. All the intracellular enzymes contain only one conserved catalytic domain with widely diversified non-catalytic amino or carboxyl termini.
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© 1994 Springer-Verlag Berlin Heidelberg
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Shen, SH., Banville, D. (1994). Protein Tyrosine Phosphatases in Signal Transduction. In: Skouteris, G.G. (eds) Liver Carcinogenesis. NATO ASI Series, vol 88. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79215-1_6
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DOI: https://doi.org/10.1007/978-3-642-79215-1_6
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