Redox regulation of protein kinases

Truong, Thu H.; Carroll, Kate S.

doi:10.3109/10409238.2013.790873

Cited by 145 publications

(109 citation statements)

References 277 publications

Supporting

Mentioning

105

Contrasting

Order By: Relevance

“…The MAPK signaling cascades, including MAPKs, are integral parts of plant biotic and abiotic stress signaling pathways and are activated by H 2 O 2 (15,16). In yeast and human model systems, MAPKs are redox-regulated through upstream regulators and through direct cysteine oxidation events (17). A cysteine oxidation event in the human p38 MAPK had been shown to act as a functional regulatory switch (18)…”

Section: Unique Sulfenylated Proteins Are Selectively Trapped With Yamentioning

confidence: 99%

See 1 more Smart Citation

Sulfenome mining in Arabidopsis thaliana

Waszczak

Akter

Eeckhout

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

166

145

View full text Add to dashboard Cite

Reactive oxygen species (ROS) have been shown to be potent signaling molecules. Today, oxidation of cysteine residues is a well-recognized posttranslational protein modification, but the signaling processes steered by such oxidations are poorly understood. To gain insight into the cysteine thiol-dependent ROS signaling in Arabidopsis thaliana, we identified the hydrogen peroxide (H 2 O 2 )-dependent sulfenome: that is, proteins with at least one cysteine thiol oxidized to a sulfenic acid. By means of a genetic construct consisting of a fusion between the C-terminal domain of the yeast (Saccharomyces cerevisiae) AP-1-like (YAP1) transcription factor and a tandem affinity purification tag, we detected ∼100 sulfenylated proteins in Arabidopsis cell suspensions exposed to H 2 O 2 stress. The in vivo YAP1-based trapping of sulfenylated proteins was validated by a targeted in vitro analysis of DEHYDROASCORBATE REDUCTASE2 (DHAR2). In DHAR2, the active site nucleophilic cysteine is regulated through a sulfenic acid-dependent switch, leading to S-glutathionylation, a protein modification that protects the protein against oxidative damage.oxidative stress | redox regulation | cysteine oxidation N umerous posttranslational modifications (PTMs) have been discovered within proteomes, creating a complex landscape of protein diversity and function (1). One of the recognized reversible redox-based PTMs is the oxidation of a cysteine thiol group to a sulfenic acid (Cys-SOH) (2) that acts as regulatory switch in several oxidative stress signal transduction pathways (3). Sulfenic acids, unless they are stabilized into the protein environment, can react rapidly with other protein thiols or with low-molecular weight thiols to form intramolecular and intermolecular disulfides. These mechanisms protect the sulfenic acids against overoxidation to sulfinic (SO 2 H) or sulfonic (SO 3 H) acid and allow sulfur oxygen signaling (2).In plants, the best-known redox regulation mechanisms are the light-dependent thiol-disulfide exchange switches in chloroplast proteins (4). Examples of other redox-regulated proteins are the transcription coactivator NONEXPRESSER OF PR GENES 1 (5), the vacuolar H + -ATPase (6), and several transcription factors (TFs), such as the AP2-type RAP2.4a (7), the G-group of basic leucine zipper TFs (8), and the TEOSINTEBRANCHED1/ CYLOIDEA/PROLIFERATING CELL FACTOR class I TFs (9). The redox relay mechanisms that bridge the signal perception to the final oxidative stress response are largely unknown. Some thiol peroxidases have an H 2 O 2 -dependent signaling function and can act as receptor and transducer (10). In yeast (Saccharomyces cerevisiae), the H 2 O 2 sensor oxidant receptor peroxidase1 (ORP1/glutathione peroxidase 3) controls, together with the transcription factor YAP1 (yeast AP-1-like), a redox regulon via a sulfenic acid thiol-disulfide relay mechanism (11). Upon reaction with H 2 O 2 , the peroxidatic cysteine of ORP1 is oxidized to a sulfenic acid that reacts with the YAP1 C-terminal cysteine-rich domain (...

show abstract

Section: Unique Sulfenylated Proteins Are Selectively Trapped With Yamentioning

confidence: 99%

“…The MAPK activity is also controlled through dephosphorylation by redox-sensitive phosphatases (17). Sulfenylation of the catalytic nucleophilic cysteine leads to the inhibition of protein tyrosine phosphatases (PTPs) (19).…”

Section: Unique Sulfenylated Proteins Are Selectively Trapped With Yamentioning

confidence: 99%

Sulfenome mining in Arabidopsis thaliana

Waszczak

Akter

Eeckhout

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

166

145

View full text Add to dashboard Cite

show abstract

“…Increased expression of AREG is responsible for activation of EGFR, but not BTC. Knockdown of EGFR in Cr(VI)- Redox homeostasis and signaling are associated with protein kinases and growth factor receptor activation (30). Previous study has documented that several agents such as radiation, oxidants, and alkylating agents induce ligand-independent activation of the EGFR (31).…”

Section: Discussionmentioning

confidence: 99%

Constitutive Activation of Epidermal Growth Factor Receptor Promotes Tumorigenesis of Cr(VI)-transformed Cells through Decreased Reactive Oxygen Species and Apoptosis Resistance Development

Kim

Dai

Fai

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Chronic exposure to Cr(VI) causes cell transformation. Results: Cr(VI)-transformed cells exhibit activated EGFR, reduced ROS generation, and development of apoptosis resistance. Conclusion: Constitutive activation of EGFR promotes tumorigenesis of Cr(VI)-transformed cells.Significance: The findings provide a new understanding on carcinogenic mechanisms of not only Cr(VI) but also other metals, such as arsenic and nickel. It also can be used to formulate cancer prevention strategies.

show abstract

“…Theirs impact is supposed to be limited in the proximity area of their formation. Instead recent evidences indicate their implications in cellular signaling suggesting that individual chemical properties of reactive species make difference in their biological role [53].…”

Section: Reactive Species In Cellular Signalingmentioning

confidence: 99%

“…Oxidative stress triggers cellular response by activating/inhibiting many signaling pathways (Figure 10). More details about the cellular response in ROS and other radical and non-radicals species attack in oxidative events can be found in [53] [56]- [60].…”

Section: Reactive Species In Cellular Signalingmentioning

confidence: 99%

Superoxide Dismutase: Therapeutic Targets in SOD Related Pathology

Filip¹,

Albu²,

Zamosteanu³

2014

Health

View full text Add to dashboard Cite

There are growing evidences on the role of adaptive mechanisms of all cell types in pathological processes: atherosclerosis, ischemic attack, bacterial infections, etc. All kinds of these processes involve as main mechanism oxidative stress. Aerobic organisms use oxygen in processes that accidentally or deliberately generate aggressive species for the biologic components in the form of radicals. Radicals were looked initially as "harmful" molecules and this is true for large quantities but in small or even moderate amounts these molecules prove to have a physiological role. Reactive species are highly reactive and as a consequence are short living species. Their impact is supposed to be limited in the proximity area of their formation. Instead recent evidences indicate their implications in cellular signaling suggesting that individual chemical properties of reactive species make a difference in their biological role. This paper presents superoxide, nitric oxide and peroxide radical generation under cellular changing conditions, the adapting behavior of the enzymes that synthesize and remove them as well as some therapeutic target in superoxide related pathology.

show abstract

Redox regulation of protein kinases

Cited by 145 publications

References 277 publications

Sulfenome mining in Arabidopsis thaliana

Sulfenome mining in Arabidopsis thaliana

Constitutive Activation of Epidermal Growth Factor Receptor Promotes Tumorigenesis of Cr(VI)-transformed Cells through Decreased Reactive Oxygen Species and Apoptosis Resistance Development

Superoxide Dismutase: Therapeutic Targets in SOD Related Pathology

Contact Info

Product

Resources

About