tailieunhanh - Báo cáo khoa học: Protein tyrosine phosphatases: regulatory mechanisms

Protein-tyrosine phosphatases are tightly controlled by various mecha-nisms, ranging from differential expression in specific cell types to restricted subcellular localization, limited proteolysis, post-translational modifications affecting intrinsic catalytic activity, ligand binding and dimerization. Here, we review the regulatory mechanisms found to control the classical pro-tein-tyrosine phosphatases. | ỊFEBS Journal MINIREVIEW Protein tyrosine phosphatases regulatory mechanisms Jeroen den Hertog1 Arne Ostman2 and Frank-D. Bohmer3 1 Hubrecht Institute Utrecht the Netherlands 2 Department of Oncology-Pathology Karolinska Institutet Stockholm Sweden 3 Institute of Molecular CellBiology Friedrich-Schiller-Universitat Jena Germany Keywords catalytic activity differential expression dimerization ligand binding oxidation phosphorylation R PTP receptor proteintyrosine phosphate regulation subcellular localization Correspondence J. den Hertog Hubrecht Institute Uppsalalaan 8 3584 CT Utrecht the Netherlands Fax 31 30 251 6464 Tel 31 30 212 1800 E-mail Protein-tyrosine phosphatases are tightly controlled by various mechanisms ranging from differential expression in specific cell types to restricted subcellular localization limited proteolysis post-translational modifications affecting intrinsic catalytic activity ligand binding and dimerization. Here we review the regulatory mechanisms found to control the classical pro-tein-tyrosine phosphatases. Received 27 October 2007 revised 10 December 2007 accepted 10 December 2007 doi Protein phosphorylation on tyrosine residues is an important cell-signaling mechanism controlled by the combined actions of protein-tyrosine kinases PTKs and protein-tyrosine phosphatases PTPs . PTKs are tightly regulated by various mechanisms. Whereas PTPs were initially regarded as household enzymes with constitutive activity dephosphorylating all the substrates they encountered evidence is now accumulating that PTPs are tightly regulated. As described elsewhere in this minireview series the human genome encodes around 100 enzymes that have the capacity to dephosphorylate phosphotyrosine pTyr in proteins 1 2 . We focus on the regulatory mechanisms of classical PTPs a cysteine-based subclass of the PTP superfamily that exclusively dephosphorylates pTyr in proteins. Classical PTPs comprise .

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