title: Redox regulation of phosphatase function.
abstract: Although reactive oxygen species play important roles in cellular physiology as signalling molecules, their molecular targets are largely unknown. A probable group of targets for mediating many of the effects of reactive oxygen species on cell signalling is the large diverse family of cysteine-dependent phosphatases, which includes the protein tyrosine phosphatases. Our work and that of others suggest that the oxidative inactivation of protein and lipid phosphatases plays an important part in signalling, downstream of many cellular stimuli. Future studies should give us a clearer picture of the role of phosphatase inactivation in cellular behaviour and explain how specificity is achieved in redox signalling.
authors.affiliation: Division of Cell Signalling, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK. n.r.leslie@dundee.ac.uk
authors.forename: N R
authors.initials: NR
authors.lastname: Leslie
authors.forename: Y
authors.initials: Y
authors.lastname: Lindsay
authors.forename: S H
authors.initials: SH
authors.lastname: Ross
authors.forename: C P
authors.initials: CP
authors.lastname: Downes
mesh_terms: D000818:Animals; D007700:Kinetics; D008954:Models, Biological; D010084:Oxidation-Reduction; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D010744:Phosphoric Monoester Hydrolases; D017027:Protein Tyrosine Phosphatases