From form to function: signaling by protein tyrosine phosphatases

Article Abstract:

Protein tyrosine phosphatases (PTPs) belong to the class of protein phosphatases which hydrolyze phosphotyrosine-specific substrates. PTPs are involved in the regulation of signal transduction pathways and are characterized by a conserved active-site sequence within the catalytic domain of approximately 240 residues. Recent findings on the function of PTPs suggest that PTPs and not protein tyrosine kinases may be the key enzymes controlling tyrosine phosphorylation.

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Redox Redux: Revisiting PTPs and the control of cell signaling

Article Abstract:

The architecture of the active site of members of the protein tyrosine phosphatase (PTP) superfamily renders these enzymes sensitive to reversible oxidation and inactivation. The importance of reversible oxidation of PTP superfamily members in controlling the signal output following an extracellular stimulus is discussed.

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A genomic and functional inventory of deubiquitinating enzymes

Article Abstract:

An inventory of the deubiquitinating enzymes encoded in the human genome is presented. Further, the literature concerning these enzymes, with particular emphasis on their function, specificity, and the regulation of their activity is reviewed.

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