SCF E3 ligase PP2-B11 plays a positive role in response to salt stress in<i>Arabidopsis</i>

Jia, Fengjuan; Chun-yan, Wang; Huang, Jinguang; Yang, Guodong; Wu, Changai; Zheng, Chengchao

doi:10.1093/jxb/erv245

Cited by 72 publications

(35 citation statements)

References 86 publications

(98 reference statements)

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“…Transcript levels for the VIP1 binding F‐box protein (AT1G56250) are upregulated by Agrobacterium tumefaciens and help to bring the transfer DNA inside the plant by degrading VirE2 and VIP1 proteins that coat the transfer DNA (Zaltsman et al, 2010). The expression of PP2‐B11 (AT1G80110) is elevated by salt stress, and overexpression lines of this gene are more tolerant to high‐salinity conditions (Jia et al, 2015). Lee et al (2014) showed that overexpression lines of PP2‐B11 are more sensitive to drought stress, suggesting that PP2‐B11 is a negative regulator in the response to drought stress.…”

Section: Resultsmentioning

confidence: 99%

Genome‐Wide Screening for Lectin Motifs in Arabidopsis thaliana

2017

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For more than three decades, served as a model for plant biology research. At present only a few protein families have been studied in detail in . This study focused on all sequences with lectin motifs in the genome of . Based on amino acid sequence similarity (BLASTp searches), 217 putative lectin genes were retrieved belonging to 9 out of 12 different lectin families. The domain organization and genomic distribution for each lectin family were analyzed. Domain architecture analysis revealed that most of these lectin gene sequences are linked to other domains, often belonging to protein families with catalytic activity. Many protein domains identified are known to play a role in stress signaling and defense, suggesting a major contribution of the putative lectins in development and plant defense. This genome-wide screen for different lectin motifs will help to unravel the functional characteristics of lectins. In addition, phylogenetic trees and WebLogos were created and showed that most lectin sequences that share the same domain architecture evolved together. Furthermore, the amino acids responsible for carbohydrate binding are largely conserved. Our results provide information about the evolutionary relationships and functional divergence of the lectin motifs in .

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Section: Resultsmentioning

confidence: 99%

Genome‐Wide Screening for Lectin Motifs in Arabidopsis thaliana

2017

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“…To understand the distribution of Na + in plant roots, 1‐week‐old roots were subjected to water and 200 mmol/L NaCl treatments for 1 d, and the distribution of Na + was detected, according to previous reports (Jia et al 2015). The roots were also treated with water and 200 mmol/L NaCl for 7 d, and the Na + and K + ion contents were determined, as previously described (Shukla et al 2012).…”

Section: Methodsmentioning

confidence: 99%

The involvement of wheat U‐box E3 ubiquitin ligase TaPUB1 in salt stress tolerance

Wang

et al. 2019

JIPB

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U-box E3 ubiquitin ligases play important roles in the ubiquitin/26S proteasome machinery and in abiotic stress responses. TaPUB1-overexpressing wheat (Triticum aestivum L.) were generated to evaluate its function in salt tolerance. These plants had more salt stress tolerance during seedling and flowering stages, whereas the TaPUB1-RNA interference (RNAi)-mediated knock-down transgenic wheat showed more salt stress sensitivity than the wild type (WT). TaPUB1 overexpression upregulated the expression of genes related to ion channels and increased the net root Na + efflux, but decreased the net K + efflux and H + influx, thereby maintaining a low cytosolic Na + /K + ratio, compared with the WT. However, RNAi-mediated knock-down plants showed the opposite response to salt stress. TaPUB1 could induce the expression of some genes that improved the antioxidant capacity of plants under salt stress. TaPUB1 also interacted with TaMP (Triticum aestivum α-mannosidase protein), a regulator playing an important role in salt response in yeast and in plants. Thus, low cytosolic Na + / K + ratios and better antioxidant enzyme activities could be maintained in wheat with overexpression of TaPUB1 under salt stress. Therefore, we conclude that the U-box E3 ubiquitin ligase TaPUB1 positively regulates salt stress tolerance in wheat.

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“…Most importantly, we proved that AtPP2-B11 negatively regulates ABA-mediated processes by specifically targeting SnRK2.3 for degradation ( Fig 1 ; Fig 3 ; S10 Fig ; S11 Fig ), and the degradation of SnRK2.3 is induced by ABA in vitro and in vivo ( Fig 4 ). AtPP2-B11 encodes an F-box protein, and previous reports have shown that AtPP2-B11 is responsive to abiotic stress and is involved in plant tolerance to drought and salt stress [ 29 , 30 ]. In this study, we showed that AtPP2-B11 was expressed in multiple tissues and organs, and that it was induced by ABA ( Fig 5 ).…”

Section: Discussionmentioning

confidence: 99%

“…In Arabidopsis , phloem protein 2-B11 (AtPP2-B11) is an F-box protein that acts as the substrate receptor for SCF type E3 ligases and which regulates LEA protein stability in drought-exposed plants [ 29 ]. AtPP2-B11 also affects the annexin1 protein level to positively regulate the response of plants to salt stress [ 30 ]. In this study, we show that AtPP2-B11 specifically targets SnRK2.3 for degradation.…”

Section: Introductionmentioning

confidence: 99%

SCFAtPP2-B11 modulates ABA signaling by facilitating SnRK2.3 degradation in Arabidopsis thaliana

et al. 2017

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The phytohormone abscisic acid (ABA) is an essential part of the plant response to abiotic stressors such as drought. Upon the perception of ABA, pyrabactin resistance (PYR)/PYR1-like (PYL)/regulatory components of ABA receptor (RCAR) proteins interact with co-receptor protein phosphatase type 2Cs to permit activation Snf1-related protein kinase2 (SnRK2) kinases, which switch on ABA signaling by phosphorylating various target proteins. Thus, SnRK2 kinases are central regulators of ABA signaling. However, the mechanisms that regulate SnRK2 degradation remain elusive. Here, we show that SnRK2.3 is degradated by 26S proteasome system and ABA promotes its degradation. We found that SnRK2.3 interacts with AtPP2-B11 directly. AtPP2-B11 is an F-box protein that is part of a SKP1/Cullin/F-box E3 ubiquitin ligase complex that negatively regulates plant responses to ABA by specifically promoting the degradation of SnRK2.3. AtPP2-B11 was induced by ABA, and the knockdown of AtPP2-B11 expression markedly increased the ABA sensitivity of plants during seed germination and postgerminative development. Overexpression of AtPP2-B11 does not affect ABA sensitivity, but inhibits the ABA hypersensitive phenotypes of SnRK2.3 overexpression lines. These results reveal a novel mechanism through which AtPP2-B11 specifically degrades SnRK2.3 to attenuate ABA signaling and the abiotic stress response in Arabidopsis.

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SCF E3 ligase PP2-B11 plays a positive role in response to salt stress inArabidopsis

Abstract: HighlightAtPP2-B11, an F-box protein, enhances the salt stress tolerance by regulating AnnAt1 expression, repressing reactive oxygen species production, and disrupting Na+ homeostasis in Arabidopsis.

Cited by 72 publications

References 86 publications

Genome‐Wide Screening for Lectin Motifs in Arabidopsis thaliana

Genome‐Wide Screening for Lectin Motifs in Arabidopsis thaliana

The involvement of wheat U‐box E3 ubiquitin ligase TaPUB1 in salt stress tolerance

SCFAtPP2-B11 modulates ABA signaling by facilitating SnRK2.3 degradation in Arabidopsis thaliana

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