title: The mechanism of protein kinase regulation by protein phosphatases.
abstract: Protein kinases are an important class of substrate of the protein phosphatases. We have examined the mechanism of dephosphorylation of the activation segments of the insulin receptor kinase and cyclin-dependent kinase 2 by their respective phosphatases, namely the tyrosine specific phosphatase PTP1B and the dual specificity phosphatase KAP. These studies reveal that PTP1B and KAP utilize contrasting mechanisms in order to dephosphorylate their substrates specifically.
authors.affiliation: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. dbarford@icr.ac.uk
authors.forename: D
authors.initials: D
authors.lastname: Barford
mesh_terms: D000818:Animals; D042846:CDC2-CDC28 Kinases; D018797:Cell Cycle Proteins; D051357:Cyclin-Dependent Kinase 2; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D018844:Cyclin-Dependent Kinases / Q000378:metabolism*; D054637:Dual-Specificity Phosphatases; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D017027:Protein Tyrosine Phosphatases; D011972:Receptor, Insulin / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D018797:Cell Cycle Proteins; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D011494:Protein Kinases; D011972:Receptor, Insulin; D017346:Protein Serine-Threonine Kinases; D042846:CDC2-CDC28 Kinases; D051357:Cyclin-Dependent Kinase 2; D018844:Cyclin-Dependent Kinases; D010749:Phosphoprotein Phosphatases; C084429:CDKN3 protein, human; D054637:Dual-Specificity Phosphatases; D017027:Protein Tyrosine Phosphatases