Elsevier

Methods in Enzymology

Volume 201, 1991, Pages 451-465
Methods in Enzymology

[39] Resolution and characterization of multiple protein-tyrosine phosphatase activities

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Publisher Summary

This chapter discusses the resolution and characterization of multiple protein-tyrosine phosphatase activities. Reversible phosphorylation of proteins on tyrosine residues is one of the earliest events in signal transduction pathways leading to the stimulation of cell proliferation. This regulatory mechanism plays a critical role in the transformation of animal cells to a tumor-like phenotype and participates in the control of other cell functions. The extent of phosphorylation of these proteins depends on the balance of the protein kinase and protein phosphatase activities toward a particular substrate protein and protein-tyrosine phosphatases (PTPs) play a critical role in regulating tyrosine phosphorylation reactions. Protein-tyrosine phosphatases can be grouped into two categories depending on whether they are part of receptor-like molecules. The sequences of three non receptor PTPs are known and they share extensive homology (30-70%) with the receptor-like PTPs within a core domain.

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