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Regulation of protein tyrosine phosphatases by reversible oxidation

Arne Ostman1, Jeroen Frijhoff, Asa Sandin

  • 1Cancer Center Karolinska, Department of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden. arne.ostman@ki.se

Journal of Biochemistry
|August 23, 2011
PubMed

Insights

Protein-tyrosine phosphatases (PTPs) are reversibly inactivated by oxidation, linking cellular signaling to reactive oxygen species (ROS). Understanding PTP oxidation mechanisms is key for future therapeutic strategies.

Area of Science:

  • Biochemistry
  • Cellular Signaling
  • Redox Biology

Background:

  • Protein-tyrosine phosphatases (PTPs) regulate tyrosine phosphorylation, a key signaling mechanism.
  • Oxidative modification of PTPs by reactive oxygen species (ROS) and reactive nitrogen species (RNS) is an emerging regulatory pathway.
  • PTP inactivation by oxidation links cellular redox state to tyrosine phosphorylation signaling.

Purpose of the Study:

  • To review recent findings on pathways, enzymes, and biochemical mechanisms of PTP oxidation.
  • To discuss the role of PTP oxidation in physiological processes and pathologies.
  • To propose criteria for establishing causal involvement of PTP oxidation.

Main Methods:

  • Literature review of recent findings on PTP oxidation.
  • Analysis of biochemical mechanisms and cellular pathways involved in PTP oxidation.
  • Examination of PTP family susceptibility and types of oxidative modification.

Main Results:

  • PTP oxidation is induced by general cellular redox state and ligand-stimulated ROS production.
  • PTPs exhibit differential susceptibility to oxidation, with various oxidative modifications possible.
  • PTP oxidation plays a role in physiological signaling and various pathologies.

Conclusions:

  • Selective PTP oxidation mechanisms require further elucidation.
  • Pharmacological modulation of PTP oxidation pathways presents a future research direction.
  • Establishing causal links between PTP oxidation and cellular processes is crucial.

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