Regulation of protein tyrosine phosphatases by reversible oxidation
TLDR
The role of PTP oxidation for physiological signalling processes as well as in different pathologies is described on the basis of well-investigated examples and criteria to establish the causal involvement of P TP oxidation in a given process are proposed.Abstract:
Oxidation of the catalytic cysteine of protein-tyrosine phosphatases (PTP), which leads to their reversible inactivation, has emerged as an important regulatory mechanism linking cellular tyrosine phosphorylation and signalling by reactive-oxygen or -nitrogen species (ROS, RNS). This review focuses on recent findings about the involved pathways, enzymes and biochemical mechanisms. Both the general cellular redox state and extracellular ligand-stimulated ROS production can cause PTP oxidation. Members of the PTP family differ in their intrinsic susceptibility to oxidation, and different types of oxidative modification of the PTP catalytic cysteine can occur. The role of PTP oxidation for physiological signalling processes as well as in different pathologies is described on the basis of well-investigated examples. Criteria to establish the causal involvement of PTP oxidation in a given process are proposed. A better understanding of mechanisms leading to selective PTP oxidation in a cellular context, and finding ways to pharmacologically modulate these pathways are important topics for future research.read more
Citations
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References
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Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation
TL;DR: The higher levels of intracellular phosphoproteins observed in cells most likely occur because of the concomitant inhibition of protein phosphatases and activation of protein kinases.
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Nox Enzymes, ROS, and Chronic Disease: An Example of Antagonistic Pleiotropy
TL;DR: It is proposed that these pathological roles of Nox enzymes can be understood in terms of antagonistic pleiotropy: genes that confer a reproductive advantage early in life can have harmful effects late in life, particularly in chronic diseases associated with an aging population.
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Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
Jaeyul Kwon,Seung-Rock Lee,Kap-Seok Yang,Younghee Ahn,Yeun Ju Kim,Earl R. Stadtman,Sue Goo Rhee +6 more
TL;DR: It is shown that H2O2 produced in response to stimulation of cells with epidermal growth factor or platelet-derived growth factor potentiates PIP3 generation and activation of the protein kinase Akt induced by these growth factors, and that peroxiredoxin likely participates in PIP2 signaling by modulating the local concentration of H2 O2.
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Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
TL;DR: The crystal structures of the regulatory sulphenic and irreversible sulphinic and sulphonic acids of protein tyrosine phosphatase 1B (PTP1B), an important enzyme in the negative regulation of the insulin receptor and a therapeutic target in type II diabetes and obesity, are reported.
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PTPσ Is a Receptor for Chondroitin Sulfate Proteoglycan, an Inhibitor of Neural Regeneration
Yingjie Shen,Alan P. Tenney,Sarah A. Busch,Kevin P. Horn,Fernando X. Cuascut,Kai Liu,Zhigang He,Jerry Silver,John G. Flanagan +8 more
TL;DR: It is shown that a transmembrane protein tyrosine phosphatase, PTPσ, binds with high affinity to neural CSPGs and may provide new therapeutic approaches to neural regeneration.