Regulation of protein tyrosine phosphatases by reversible oxidation
Reads0
Chats0
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
More filters
Journal ArticleDOI
Ferroptosis at the crossroads of cancer-acquired drug resistance and immune evasion.
TL;DR: An overview of the known mechanisms that regulate sensitivity to ferroptosis in cancer cells and how the modulation of metabolic pathways controlling ferroPTosis might reshape the tumour niche, leading to an immunosuppressive microenvironment that promotes tumour growth and progression is provided.
Journal ArticleDOI
Mitochondrial reactive oxygen species and cancer
TL;DR: In this article, the authors discuss how cancer-associated mutations and microenvironments can increase production of reactive oxygen species (mROS), which can lead to activation of tumorigenic signaling and metabolic reprogramming.
Journal ArticleDOI
Drug-induced oxidative stress and toxicity.
TL;DR: The nature of ROS-induced damage on key cellular targets of oxidative stress is examined and evidence implicating ROS in clinically relevant, drug-related side effects including doxorubicin-induced cardiac damage, azidothymidine-induced myopathy, and cisplatin-induced ototoxicity is reviewed.
Journal ArticleDOI
Mitochondria as a Source of Reactive Oxygen and Nitrogen Species: From Molecular Mechanisms to Human Health
Tiago R. Figueira,Mario H. Barros,Anamaria A. Camargo,Roger F. Castilho,Julio C.B. Ferreira,Alicia J. Kowaltowski,Francis Sluse,Nadja C. de Souza-Pinto,Anibal E. Vercesi +8 more
TL;DR: The interaction between mitochondrial reactive oxygen and nitrogen species, and the involvement of these oxidants in mitochondrial diseases, cancer, neurological, and cardiovascular disorders are discussed.
Journal ArticleDOI
Oxidant Sensing by Reversible Disulfide Bond Formation
Claudia M. Cremers,Ursula Jakob +1 more
TL;DR: Maintenance of the cellular redox balance is crucial for cell survival and has the potential to mediate extensive yet fully reversible structural and functional changes, rapidly adjusting the protein's activity to the prevailing oxidant levels.
References
More filters
Journal ArticleDOI
Protein-tyrosine phosphatases and cancer
TL;DR: An improved understanding of how tyrosine phosphorylation function and how they are regulated might aid the development of new anticancer agents.
Journal ArticleDOI
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
TL;DR: It is shown that PrxI associated with membranes is transiently phosphorylated on tyrosine-194 and thereby inactivated both in cells stimulated via growth factor or immune receptors in vitro and in those at the margin of healing cutaneous wounds in mice.
Journal ArticleDOI
Reactive oxygen species enhance insulin sensitivity.
Kim Loh,Haiyang Deng,Atsushi Fukushima,Xiaochu Cai,Benoit Boivin,Sandra Galic,Clinton R. Bruce,Benjamin J. Shields,Beata Skiba,Lisa M Ooms,Nigel K. Stepto,Ben Jing Wu,Christina Anne Mitchell,Nicholas K. Tonks,Matthew J. Watt,Mark A. Febbraio,Peter J Crack,Sofianos Andrikopoulos,Tony Tiganis +18 more
TL;DR: In this article, the authors reported that mice lacking one of the key enzymes involved in the elimination of physiological ROS, glutathione peroxidase 1 (Gpx1), were protected from high-fat-diet-induced insulin resistance.
Journal ArticleDOI
Insulin-stimulated Hydrogen Peroxide Reversibly Inhibits Protein-tyrosine Phosphatase 1B in Vivo and Enhances the Early Insulin Action Cascade
TL;DR: It is shown that insulin stimulation generates a burst of intracellular H2O2 in insulin-sensitive hepatoma and adipose cells that is associated with reversible oxidative inhibition of up to 62% of overall cellular PTPase activity, as measured by a novel method using strictly anaerobic conditions.
Journal ArticleDOI
Regulation of ROS signal transduction by NADPH oxidase 4 localization
TL;DR: It is demonstrated that nicotinamide adenine dinucleotide phosphate reduced oxidase 4 (Nox4), a major Nox isoform expressed in nonphagocytic cells, including vascular endothelium, is localized to the endoplasmic reticulum (ER), indicating that the specificity of intracellular ROS-mediated signal transduction may be modulated by the localization of Noxisoforms within specific subcellular compartments.