Protein Promiscuity in H<sub>2</sub>O<sub>2</sub>Signaling

Young, Diana; Pedre, Brandán; Ezeriņa, Daria; Smet, Barbara De; Lewandowska, Aleksandra; Tossounian, Maria-Armineh; Bodra, Nandita; Huang, Jingjing; Rosado, Leonardo Astolfi; Breusegem, Frank Van; Messens, Joris

doi:10.1089/ars.2017.7013

Cited by 28 publications

(21 citation statements)

References 430 publications

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“…Although some cysteines can be directly oxidized by H 2 O 2, most of them require prior activation to be deprotonated, involving additional redox-sensitive relays. The best candidates for this relay function appear to be proteins first identified as antioxidant safe-guarders [ 30 , 31 , 32 , 33 , 34 , 35 , 36 ] reviews in [ 37 , 38 , 39 , 40 , 41 ], and they will be discussed below. It is now clear that the role of H 2 O 2 signalling in oxidative eustress has to integrate the entire redox machine.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen Peroxide and Redox Regulation of Developments

et al. 2018

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Reactive oxygen species (ROS), which were originally classified as exclusively deleterious compounds, have gained increasing interest in the recent years given their action as bona fide signalling molecules. The main target of ROS action is the reversible oxidation of cysteines, leading to the formation of disulfide bonds, which modulate protein conformation and activity. ROS, endowed with signalling properties, are mainly produced by NADPH oxidases (NOXs) at the plasma membrane, but their action also involves a complex machinery of multiple redox-sensitive protein families that differ in their subcellular localization and their activity. Given that the levels and distribution of ROS are highly dynamic, in part due to their limited stability, the development of various fluorescent ROS sensors, some of which are quantitative (ratiometric), represents a clear breakthrough in the field and have been adapted to both ex vivo and in vivo applications. The physiological implication of ROS signalling will be presented mainly in the frame of morphogenetic processes, embryogenesis, regeneration, and stem cell differentiation. Gain and loss of function, as well as pharmacological strategies, have demonstrated the wide but specific requirement of ROS signalling at multiple stages of these processes and its intricate relationship with other well-known signalling pathways.

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Section: Introductionmentioning

confidence: 99%

Hydrogen Peroxide and Redox Regulation of Developments

et al. 2018

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“…Oxidative protein modifications, such as sulfenylation, sulfinylation and sulfonylation, as well as intra- and inter-molecular disulfide bond formation, are rapid and reversible mechanisms (except irreversible sulfonylation) to regulate protein function in living cells in response to changing redox states [32]. Sulfur-containing amino acids such as cysteine are highly susceptible to oxidation by ROS such as H 2 O 2 .…”

Section: Post-translational Modification Of Peroxisomal Proteinsmentioning

confidence: 99%

“…Mass spectrometry-based techniques and proteomics have been used to identify sulfenylated proteins in plants (for review see [33]). A biotin switch method originally designed to detect protein S -nitrosylation has been adapted by changing the reducing agent from ascorbate to arsenite in order to identify sulfenylated proteins (for review see [32]). Western blot analysis using an anti-cysteine sulfenic acid antibody also enables sulfenylated proteins to be identified [36].…”

Section: Post-translational Modification Of Peroxisomal Proteinsmentioning

confidence: 99%

Multilevel Regulation of Peroxisomal Proteome by Post-Translational Modifications

Sandalio

Gotor

Romero

et al. 2019

IJMS

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Peroxisomes, which are ubiquitous organelles in all eukaryotes, are highly dynamic organelles that are essential for development and stress responses. Plant peroxisomes are involved in major metabolic pathways, such as fatty acid β-oxidation, photorespiration, ureide and polyamine metabolism, in the biosynthesis of jasmonic, indolacetic, and salicylic acid hormones, as well as in signaling molecules such as reactive oxygen and nitrogen species (ROS/RNS). Peroxisomes are involved in the perception of environmental changes, which is a complex process involving the regulation of gene expression and protein functionality by protein post-translational modifications (PTMs). Although there has been a growing interest in individual PTMs in peroxisomes over the last ten years, their role and cross-talk in the whole peroxisomal proteome remain unclear. This review provides up-to-date information on the function and crosstalk of the main peroxisomal PTMs. Analysis of whole peroxisomal proteomes shows that a very large number of peroxisomal proteins are targeted by multiple PTMs, which affect redox balance, photorespiration, the glyoxylate cycle, and lipid metabolism. This multilevel PTM regulation could boost the plasticity of peroxisomes and their capacity to regulate metabolism in response to environmental changes.

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“…are even more reactive towards H 2 O 2 with a rate constant 10 4 to 10 6 higher than proteins bearing low pKa cysteine [42], and they emerge as essential for redox relay [36]. The activity of these enzymes is also subject to regulation [43].…”

Section: The Redox Machinementioning

confidence: 99%

“…Although some cysteines can be directly oxidized by H 2 O 2, most of them require prior activation to be deprotonated, involving additional redox-sensitive relays. The best candidates for this relay function appear to be proteins first identified as antioxidant safe-guarders [25][26][27][28][29][30][31] reviews in [32][33][34][35][36], and they will be discussed below. It is now clear that the role of H 2 O 2 signalling in oxidative eustress has to integrate the entire redox machine.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen Peroxide and Redox Regulation of Development

Rampon¹,

Volovitch²,

Joliot³

et al. 2018

Preprint

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Reactive oxygen species (ROS), which were originally classified as exclusively deleterious compounds, have gained increasing interest in the recent years given their action as bona fide signalling molecules. The main target of ROS action is the reversible oxidation of cysteines, leading to the formation of disulfide bonds, which modulate protein conformation and activity. ROS endowed with signalling properties are mainly produced by NADPH oxidases at the plasma membrane, but their action also involves a complex machinery of multiple redox-sensitive protein families that differs in their subcellular localization and their activity. Given that the levels and distribution of ROS are highly dynamic in part due to their limited stability, the development of various fluorescent ROS sensors, some of which are quantitative (ratiometric), represents a clear breakthrough in the field and have been adapted to both ex vivo and in vivo applications. The physiological implication of ROS signalling will be presented mainly in the frame of morphogenetics processes, embryogenesis, regeneration, and stem cell differentiation. Gain and loss of function as well as pharmacological strategies have demonstrated the wide but specific requirement of ROS signalling at multiple stages of these processes and its intricate relationship with other well-known signalling pathways.

show abstract

Protein Promiscuity in H₂O₂Signaling

Cited by 28 publications

References 430 publications

Hydrogen Peroxide and Redox Regulation of Developments

Hydrogen Peroxide and Redox Regulation of Developments

Multilevel Regulation of Peroxisomal Proteome by Post-Translational Modifications

Hydrogen Peroxide and Redox Regulation of Development

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Protein Promiscuity in H2O2Signaling

Cited by 28 publications

References 430 publications

Hydrogen Peroxide and Redox Regulation of Developments

Hydrogen Peroxide and Redox Regulation of Developments

Multilevel Regulation of Peroxisomal Proteome by Post-Translational Modifications

Hydrogen Peroxide and Redox Regulation of Development

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Protein Promiscuity in H₂O₂Signaling