Cyclophilin 20-3 relays a 12-oxo-phytodienoic acid signal during stress responsive regulation of cellular redox homeostasis

Park, Sang-Wook; Li, Wei; Viehhauser, Andrea; He, Bin; Park, Jae Hyeon; Nilsson, Anders; Andersson, Mats X.; Kittle, Joshua D.; Ambavaram, Madana M.R.; Luan, Sheng; Esker, Alan R.; Tholl, Dorothea; Cimini, Daniela; Ellerström, Mats; Coaker, Gitta; Mitchell, Thomas K.; Pereira, Andy; Dietz, Karl‐Josef; Lawrence, Christopher B.

doi:10.1073/pnas.1218872110

Cited by 196 publications

(225 citation statements)

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“…CYP have been found to be involved in the signalling of several phytohormones, including auxin, brassinosteroid, gibberellic acid (GA) and jasmonic acid 16,17,[23][24][25][41][42][43] . Among these and other phytohormones, the activation of the signalling pathways of GA, jasmonic acid and strigolactone also utilize a derepression mechanism by the proteasomal degradation of specific repressors in a manner similar to that of auxin [44][45][46][47][48] .…”

Section: Discussionmentioning

confidence: 99%

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

et al. 2015

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In plants, auxin signalling is initiated by the auxin-promoted interaction between the auxin receptor TIR1, an E3 ubiquitin ligase, and the Aux/IAA transcriptional repressors, which are subsequently degraded by the proteasome. Gain-of-function mutations in the highly conserved domain II of Aux/IAAs abolish the TIR1-Aux/IAA interaction and thus cause an auxin-resistant phenotype. Here we show that peptidyl-prolyl isomerization of rice OsIAA11 catalysed by LATERAL ROOTLESS2 (LRT2), a cyclophilin-type peptidyl-prolyl cis/trans isomerase, directly regulates the stability of OsIAA11. NMR spectroscopy reveals that LRT2 efficiently catalyses the cis/trans isomerization of OsIAA11. The lrt2 mutation reduces OsTIR1-OsIAA11 interaction and consequently causes the accumulation of a higher level of OsIAA11 protein. Moreover, knockdown of the OsIAA11 expression partially rescues the lrt2 mutant phenotype in lateral root development. Together, these results illustrate cyclophilincatalysed peptidyl-prolyl isomerization promotes Aux/IAA degradation, as a mechanism regulating auxin signalling.

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Section: Discussionmentioning

confidence: 99%

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

et al. 2015

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“…Preferential expression of genes upon OPDA treatment such as ZAT10 or GRX480 together with about 150 genes have been postulated repeatedly, 18,26,28 and also proteomic approaches showed OPDA-specific responses. 27 In all these experiments, however, putative formation of JA upon OPDA treatment was not excluded.…”

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confidence: 97%

“…26 GRX480 encodes a GLUTAREDOXIN and is regarded as candidate for an OPDAassociated transcription regulator. 18 Both genes were previously shown to be OPDA-inducible, 18,26 indicating their role as a putative marker for OPDA responses. COI1-independent expression was confirmed for GRX480, since tests with the coi1-16 mutant showed an OPDA-inducible expression of GRX480.…”

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confidence: 99%

“…15,16 ). Among such processes in Arabidopsis thaliana are seed germination, 17 glutathione conjugation, 18 drought stress responses, 19 and other plant defense reactions. 20 Additionally, seed formation in tomato is regulated by OPDA.…”

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confidence: 99%

“…26 Such transcriptomics data, indicating an OPDA-specificity, as well as proteomics data on OPDA-specific upregulated proteins, have been subsequently collected several times. 18,27,28 The reason for inactivity of OPDA in promoting interaction of COI1-JAZ1 or COI1-JAZ3 2,11 could be that -similar to JAthe conjugation with Ile is required. In subsequent interaction studies, however, of COI1 and JAZ1 or JAZ3, also OPDA-Ile did not induce the interaction.…”

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OPDA-Ile – a new JA-Ile-independent signal?

Wasternack

Hause

2016

Plant Signaling & Behavior

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Expression takes place for most of the jasmonic acid (JA)-induced genes in a COI1-dependent manner via perception of its conjugate JA-Ile in the SCF COI1 -JAZ co-receptor complex. There are, however, numerous genes and processes, which are preferentially induced COI1-independently by the precursor of JA, 12-oxophytodienoic acid (OPDA). After recent identification of the Ile-conjugate of OPDA, OPDA-Ile, biological activity of this compound could be unequivocally proven in terms of gene expression. Any interference of OPDA, JA, or JAIle in OPDA-Ile-induced gene expression could be excluded by using different genetic background. The data suggest individual signaling properties of OPDA-Ile. Future studies for analysis of an SCF COI1 -JAZ co-receptorindependent route of signaling are proposed. Ten years ago, the new family of JASMONATE ZIM DOMAIN (JAZ) proteins with 12 members was occasionally identified in Arabidopsis in 3 different labs. [1][2][3] This was a breakthrough in JA research, since JAZ proteins were characterized as repressors of JA-Ile-induced gene expression. With identification of these proteins, it became clear that JA-Ile is perceived by the SCF COI1 -JAZ co-receptor complex. Components of this complex are the F-box protein called CORONATINE INSENSI-TIVE 1 (COI1), the Skp1/Cullin/complex with E3 ubiquitin ligase activity and the targets of the F-box protein, the JAZ proteins. JAZ proteins repress in the absence of JA-Ile positively acting transcription factors (TFs), such as MYC2, which bind to JA responsive elements (G-boxes) in the promoters of JAIle-regulated genes. Upon stress or developmentally regulated processes, an increase in JA-Ile level occurs leading to its binding in the SCF COI1 -JAZ co-receptor complex followed by proteasomal degradation of JAZ. Consequently, the free, positively acting MYC2 can switch on JA-Ile-responsive gene expression. 4 This basic scenario could be explained mechanistically upon crystallization of the complex, where an inositol-pentakisphosphate (IP 5 ) activates JA-Ile binding. 5 Interaction of the F-box protein COI1 and one of the JAZ proteins requires the C-terminal jas domain of JAZ. 6 This interaction is promoted by JA-Ile. Among the various stereo-isomeric forms of JA-Ile, the (+)-7-iso-JA-Ile has the highest activity. 7 JA-Ile perception via the SCF COI1 -JAZ-co-receptor complex was confirmed in the last couple of years including identification of new co-repressors and adaptors (for reviews, see refs. [8][9][10] ).There is, however, one open question due to the structural specificity in binding of the ligand JA-Ile. Among 40 different jasmonate compounds the stereoisomer (+)-7-iso-JA-Ile, carrying a ring conformation similar to coronatine, was most active. 7 Even coronatine was 10-fold more active then JA-Ile, although this bacterial toxin does not occur in plants. For the methyl ester of JA, for 12-oxo-phytodienoic acid (OPDA, the precursor of JA biosynthesis), and for OPDA-Ile (Fig. 1) no detectable promotion of JAZ3-COI1 interaction was recorded...

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Jasmonic Acid Signalling

Roberts

2016

Encyclopedia of Life Sciences

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Jasmonic acid (JA) is an important plant hormone involved in the regulation of plant development and stress responses. A central feature of JA signalling is the repression of JA responses by the JASMONATE ZIM‐DOMAIN (JAZ) protein family. JAZ proteins function to inhibit the activity of transcription factors responsible for driving the expression of JA‐responsive target genes. This is achieved by recruitment of transcriptional repressors and chromatin remodelling proteins. Perception by a COI1‐JAZ coreceptor of the main bioactive molecule in JA signalling, jasmonoyl‐ l ‐isoleucine, results in JAZ protein degradation and release of JA responses from suppression. Specificity in JA signalling is generated by a combination of JAZ protein diversity, cell specificity of JA‐responsive transcription factors and interactions with other plant hormone signalling pathways. Key Concepts (+)‐7‐iso‐jasmonoyl‐ l ‐isoleucine (JA‐Ile) is the main biologically active compound responsible for jasmonic acid (JA) signalling in higher plants. JASMONATE ZIM‐DOMAIN (JAZ) proteins function as the central regulators of jasmonate signalling. JAZ proteins recruit transcriptional repressors to inhibit the activity of transcription factors that positively regulate JA responses. The F‐box protein COI1 functions along with JAZ proteins as a JA‐Ile coreceptor that controls JA‐dependent JAZ protein degradation. Specificity in JA signalling is conferred by context‐specific interactions between JAZ proteins and their targets, and by interactions between JA and other signalling pathways. There are two major pathways for jasmonate‐dependent plant defence responses, which are controlled by antagonistic master‐regulator transcription factors. Herbivores, pathogens and symbiotic microorganisms can manipulate jasmonate signalling for their own benefit. Interactions between JAZ and DELLA proteins mediate trade‐offs between growth and defence. Jasmonates likely function as long‐distance defence signals within, and possibly even between, plants. Other bioactive jasmonates include 12‐oxo‐phytodienoic acid (OPDA) and cis ‐jasmone.

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Cyclophilin 20-3 relays a 12-oxo-phytodienoic acid signal during stress responsive regulation of cellular redox homeostasis

Cited by 196 publications

References 46 publications

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

OPDA-Ile – a new JA-Ile-independent signal?

Jasmonic Acid Signalling

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