DWARF 53 acts as a repressor of strigolactone signalling in rice

Jiang, Liang; Liu, Xue; Xiong, Guosheng; Liu, Huihui; Chen, Fulu; Wang, Lei; Meng, Xiangbing; Liu, Guifu; Yu, Hong; Yuan, Yundong; Yi, Wei; Zhao, Lihua; Ma, Honglei; He, Yuanzheng; Wu, Zhongshan; Melcher, Karsten; Qian, Qian; Xu, Hui; Wang, Yonghong; Li, Jiayang

doi:10.1038/nature12870

Cited by 708 publications

(880 citation statements)

References 48 publications

(70 reference statements)

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“…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] . Interestingly, a GA-insensitive dwarf (gaid) mutant of wheat was characterized to be insensitive to exogenous GA, correlated to the elevated levels of the GA signalling repressor Rht/DELLA protein and a putative cyclophilin TaCYP20-2 protein.…”

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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“…GR24 can induce an interaction between D14 and D3, which has been shown in cells by yeast 2-hybrid analysis [25] and in extracts by pull-down assays [19,20]. To test whether GR24 directly stimulates an interaction between D14 and D3 in vitro, and to quantitatively analyze such an interaction, we used highly purified recombinant proteins in an AlphaScreen luminescence proximity assay.…”

Section: Binding Of Gr24 Inside Of the D14 Lbp Is Required For The Inmentioning

confidence: 99%

“…Recent studies have identified the putative transcriptional repressor D53 [19,20] as well as the transcription factor BES1 as SCF D3 substrate targets in response to SL exposure and the D53 paralog SMAX1 in response to karrikin exposure. SLs induce association of D14 with D3/D53 and D3/BES1 complexes and promote SCF D3 -mediated degradation of D53 [19,20], BES1 [21], and D14 itself [22].…”

Section: Introductionmentioning

confidence: 99%

Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3

et al. 2015

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Strigolactones (SLs) are endogenous hormones and exuded signaling molecules in plant responses to low levels of mineral nutrients. Key mediators of the SL signaling pathway in rice include the α/β-fold hydrolase DWARF 14 (D14) and the F-box component DWARF 3 (D3) of the ubiquitin ligase SCF D3 that mediate ligand-dependent degradation of downstream signaling repressors. One perplexing feature is that D14 not only functions as the SL receptor but is also an active enzyme that slowly hydrolyzes diverse natural and synthetic SLs including GR24, preventing the crystallization of a binary complex of D14 with an intact SL as well as the ternary D14/SL/D3 complex. Here we overcome these barriers to derive a structural model of D14 bound to intact GR24 and identify the interface that is required for GR24-mediated D14-D3 interaction. The mode of GR24-mediated signaling, including ligand recognition, hydrolysis by D14, and ligand-mediated D14-D3 interaction, is conserved in structurally diverse SLs. More importantly, D14 is destabilized upon the binding of ligands and D3, thus revealing an unusual mechanism of SL recognition and signaling, in which the hormone, the receptor, and the downstream effectors are systematically destabilized during the signal transduction process.

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“…SL degrades the D53 protein in rice [4,5] and the related SMXL6, SMXL7 and SMXL8 proteins in Arabidopsis [1]. D53 directly prevents the transcriptional activation function of IPA1 (OsSPL14) in rice [2] and the related SPL3 and SPL17 proteins in wheat [8]; D53 prevents IPA1 upregulation of D53 gene expression in rice [2], and TaSPL3 upregulation of TaTB1 gene expression in wheat [8].…”

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confidence: 99%

“…This interaction with D53 prevented the transcriptional activation activity of IPA1 in a dose-dependent manner (Figure 1). In rice, D53 is one of the only known transcriptional targets of SL [4,5], and D53 prevented IPA1 from upregulating D53 expression [2] ( Figure 1). By showing evidence of a mechanism via which SL signaling transcriptionally regulates downstream target genes, this work has enabled description of a continuous SL signaling pathway from perception to gene regulation ( Figure 1).…”

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confidence: 99%