12-oxo-phytodienoic acid interaction with cyclophilin CYP20-3 is a benchmark for understanding retrograde signaling in plants

Kopriva, Stanislav

doi:10.1073/pnas.1307482110

Cited by 12 publications

(9 citation statements)

References 24 publications

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“…CYP4 was identified to interact with 12-oxo-phytodienoic acid and links 12-oxophytodienoic acid signaling to amino acid biosynthesis and cellular redox homeostasis in response to stress (51). Upon interaction, the formation of a complex with O-acetylserine (thiol) lyase B and cysteine synthase is triggered, leading to an increase of thiol metabolites and the buildup of the cellular reduction potential (52).…”

Section: Figmentioning

confidence: 99%

Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress

Jacques

Ghesquière

Bock

et al. 2015

Molecular & Cellular Proteomics

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Reactive oxygen species such as hydrogen peroxide can modify proteins via direct oxidation of their sulfur-containing amino acids, cysteine and methionine. Methionine oxidation, studied here, is a reversible posttranslational modification that is emerging as a mechanism by which proteins perceive oxidative stress and function in redox signaling. Identification of proteins with oxidized methionines is the first prerequisite toward understanding the functional effect of methionine oxidation on proteins and the biological processes in which they are involved. Here, we describe a proteome-wide study of in vivo proteinbound methionine oxidation in plants upon oxidative stress using Arabidopsis thaliana catalase 2 knock-out plants as a model system. We identified over 500 sites of oxidation in about 400 proteins and quantified the differences in oxidation between wild-type and catalase 2 knock-out plants. We show that the activity of two plantspecific glutathione S-transferases, GSTF9 and GSTT23, is significantly reduced upon oxidation. And, by sampling over time, we mapped the dynamics of methionine oxidation and gained new insights into this complex and dy-

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Section: Figmentioning

confidence: 99%

Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress

Jacques

Ghesquière

Bock

et al. 2015

Molecular & Cellular Proteomics

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“…It is concluded that CYP20-3 is a key effecter linking the JA signaling pathway to the cellular redox homeostasis in stress responses It is proposed that CYP20-3 binds to 2-CysPrx and form a CYP20-3/2-CysPrx complex under normal conditions; but during stress, an increased level of OPDA is generated, and it binds CYP20-3 and releases CYP20-3 from the CYP20-3/2-CysPrx complex, then the OPDA-binding CYP20-3 recruits SAT1 to form CSC. Finally, buildup of cellular reduction potential triggered by OPDA/CYP20-3 binding reverses the conformational states of 2-CysPrx and/or CYP20-3, which leads to the reformation of CYP20-3/2-CysPrx complex Kopriva 2013 ).…”

Section: Cyclophilin 20-3 (Roc 4)mentioning

confidence: 99%

Elucidation of Abiotic Stress Signaling in Plants

Pandey¹

2015

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The above image represents a depiction of activation of different signaling pathways by diverse stimuli that converge to activate intricate signaling and interaction networks to counter stress (top panel). Since environmental stresses infl uence most signifi cantly to the reduction in potential crop yield, progress is now largely anticipated through functional genomics studies in plants through the use of techniques such as large-scale analysis of gene expression pattern in response to stress and construction, analysis and use of plant protein interactome networks maps for effective engineering strategies to generate stress tolerant crops (top panel). The molecular aspects of these signaling pathways are extensively studied in model plant Arabidopsis thaliana and crop plant rice ( Oryza sativa ) (below).

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“…It is concluded that CYP20-3 is a key effecter linking the JA signaling pathway to the cellular redox homeostasis in stress responses (Park et al 2013 ) It is proposed that CYP20-3 binds to 2-CysPrx and form a CYP20-3/2-CysPrx complex under normal conditions; but during stress, an increased level of OPDA is generated, and it binds CYP20-3 and releases CYP20-3 from the CYP20-3/2-CysPrx complex, then the OPDA-binding CYP20-3 recruits SAT1 to form CSC. Finally, buildup of cellular reduction potential triggered by OPDA/CYP20-3 binding reverses the conformational states of 2-CysPrx and/or CYP20-3, which leads to the reformation of CYP20-3/2-CysPrx complex (Park et al 2013 ;Kopriva 2013 ).…”

Section: Cyclophilin 20-3 (Roc 4)mentioning

confidence: 99%

“…As a result, removal of repressors relieves inhibition of a specifi c set of JA-responsive transcription factors and activates JA-responsive gene expression. The mechanism of JA signaling seems well understood, but there are some certain JA-regulated genes that are not COI1-dependent, leading to the speculation that there is an alternative JA signaling pathway, in addition to the COI1-dependent cascade (Kopriva 2013 ). Identifi cation of chloroplast AtCYP20-3 as a JA receptor not only confi rms the existence of the alternative JA signaling pathway, also connects JA signaling pathway with chloroplast retrograde signaling, sulfur metabolism, and redox regulation (Park et al 2013 ).…”

Section: Cyclophilin 20-3 (Roc 4)mentioning

confidence: 99%

Plant Immunophilins: A Protein Family with Diverse Functions Beyond Protein Folding Activity

Shi¹,

Fu²

2015

Elucidation of Abiotic Stress Signaling in Plants

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Immunophilins were discovered as cellular receptors for immunosuppressive drugs: cyclosporine A and FK506. Cyclophilins (CYPs, receptors for cyclosporine A) and FK506-binding proteins (FKBPs, receptors for FK506) do not share sequence homology, but have a common feature of peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the cis-trans conversion of X-Pro peptide bonds, a rate-limiting step in the process of protein folding. Immunophilins are widely present in organisms from bacteria and fungi, to animals and plants. Genomics studies revealed that plants possess the largest immunophilin family. However, the physiological function of plant immunophilins is poorly understood. In this review, starting with a brief introduction of the immunophilin family and the current knowledge about their physiological roles in diverse organisms, the recent advances in the elucidation of plant immunophilin's physiological roles, largely via functional genomics tools, are summarized here. Notably, a striking feature of plant immunophilins is that a large fraction is localized in the chloroplast. Recent studies reveal that chloroplast immunophilins play a central role in the assembly and maintenance of photosynthetic complexes.

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12-oxo-phytodienoic acid interaction with cyclophilin CYP20-3 is a benchmark for understanding retrograde signaling in plants

Cited by 12 publications

References 24 publications

Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress

Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress

Elucidation of Abiotic Stress Signaling in Plants

Plant Immunophilins: A Protein Family with Diverse Functions Beyond Protein Folding Activity

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