CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis

Yu, Zipeng; Zhang, Di; Xu, Yang; Jin, S.; Zhang, Lei; Zhang, Shizhong; Yang, Guodong; Huang, Jinguang; Ke, Yan; Wu, Changai; Zheng, Chengchao

doi:10.1093/jxb/erz302

Cited by 74 publications

(103 citation statements)

References 49 publications

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“…These results indicated that NRT1.2 enhanced ABA signaling. In contrast, a previous study indicated that CEPR2 inhibited ABA signaling(Yu et al, 2019), suggesting that CEPR2 might negatively regulate NRT1.2.…”

Section: Resultsmentioning

confidence: 64%

“…To investigate the regulatory mechanisms underlying the response of CEPR2 to ABA, we compared the phosphoproteomes of wild-type (WT) Arabidopsis seedlings to those of CEPR2-OE-9, a previously described Arabidopsis line overexpressing CEPR2 (Yu et al, 2019). We identified 169 differentially expressed phosphopeptides ( p ≤ 0.05 and fold-change ≥ 1.20 or ≤ 0.8), of which 97 (belong to 78 proteins) were upregulated and 72 (belong to 68 proteins) were downregulated (Supplementary Excel 1).…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, NRT1.2 might be phosphorylated by the kinase domain of CEPR2. To text this, we carried out MbSUS assay using the cytosol loop region of NRT1.2 (NRT1.2 loop ) and series constructs used in the previous report (Yu et al, 2019). The results indicated that the NRT1.2 loop interacted with the kinase domain of CEPR2 (CEPR2 KD ) (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Similarly, early flowering 1-like (AEL) phosphorylates PYLs to promote PYL ubiquitination and degradation, resulting in the blockage of ABA signaling and the resumption of plant growth (Chen et al, 2018). Recently, we showed that CEPR2 also phosphorylates PYLs to promote PYLs degradation, similarly leading to the suppression of the ABA response under non-stress conditions (Yu et al, 2019). Here, we found that CEPR2 phosphorylated the ABA transporter NRT1.2 and promoted NRT1.2 degradation under normal conditions (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…In response to environmental stress, ABA accumulates rapidly and is transported from the site of synthesis to the site of action, where it is recognized by ABA receptors in the pyrabactin resistance 1 family (PYR1); these proteins are also referred to as PYR1-like (PYL) (Boursiac et al, 2013). C-terminally encoded peptide receptor 2 (CEPR2), which is a typical leucine-rich repeat receptor-like kinase (LRR-RLK), controls the interaction between plant growth and the stress response in Arabidopsis by regulating the phosphorylation and degradation of ABA-receptor PYLs in response to environmental conditions (Yu et al, 2019). However, the mechanisms in CEPR2-mediated ABA response need further investigation.…”

Section: Introductionmentioning

confidence: 99%

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The stability and ABA import activity of NRT1.2 inArabidopsisare regulated by CEPR2 via phosphorylation modification

Zhang

et al. 2020

Preprint

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ABA signaling and transport play important roles in plant systematic responses to environmental factors. Previously, we reported that C-terminally encoded peptide receptor 2 (CEPR2) balances plant growth and ABA responses by phosphorylating abscisic acid (ABA) receptors. Here, we showed that CEPR2 also directly phosphorylated the ABA transporter NRT1.2 by phosphaproteomics analysis using CEPR2 overexpression line and by physiological and biochemical experiments. Using transgenic seedlings, we demonstrated that NRT1.2 positively regulated the ABA response, and that CEPR2 acted on NRT1.2 epistatically. Specifically, CEPR2 phosphorylated NRT1.2 at serine 292 (Ser292) to promote the degradation of NRT1.2 via the 26S proteasome and vacuolar degradation pathways. However, ABA strongly inhibited the phosphorylation of NRT1.2 at Ser292, stabilizing NRT1.2. Transportation assays in yeast and Xenopus oocytes showed that the nonphosphorylation of NRT1.2 showed high ABA but very low nitrate import activity, while the phosphorylation of NRT1.2 by CEPR2 eliminated NRT1.2-mediated ABA import but slightly increased nitrate transport. These findings were consistent with our analyses of complement mutants in planta. Thus, our results provide detailed mechanisms of NRT1.2 in transporting ABA and nitrate in response to environmental conditions in plants. Besides, it is a better way for plants to overexpress the unphosphorylated NRT1.2 at Ser292 both under high and low nitrate conditions.

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Section: Resultsmentioning

confidence: 64%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The stability and ABA import activity of NRT1.2 inArabidopsisare regulated by CEPR2 via phosphorylation modification

Zhang

et al. 2020

Preprint

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Abscisic Acid Regulates Fleshy Fruit Ripening and Stress Resistance

Yuan

Leng

2020

Annual Plant Reviews Online

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Abscisic acid (ABA) is an essential endogenous messenger during plant development and in stress responses. Recently, the role of ABA in both climacteric and nonclimacteric fruit ripening regulation was revealed. However, the genetic, molecular and physiological mechanisms of ABA in fruit ripening regulation is still not completely understood. ABA is involved in a wide range of fruit development processes, including fruit ripening onset, ripening process and fruit quality trait. In addition, ABA plays a significant role in responses to abiotic stress and the promotion of water efficiency in fruit. The biological effect of ABA depends on its concentration and signal transduction. This article summarises the latest discoveries of the roles of ABA in fruit development and ripening as well as in responses to abiotic stress.

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Silencing suppressors of rice black‐streaked dwarf virus and rice stripe virus hijack the 26S proteasome of Laodelphax striatellus to facilitate virus accumulation and transmission

Liu

Zhu

Gao

et al. 2022

Pest Management Science

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BACKGROUND: Rice black-streaked dwarf virus (RBSDV) is transmitted by small brown planthopper (Laodelphax striatellus [L. striatellus]) and causes devastating disease in rice. P9-1 has silencing suppression activity and is the key protein for viroplasm formation in RBSDV-infected plants and insects; however, its exact function is poorly understood.RESULTS: In this study, the P9-1 of RBSDV interacted with L. striatellus 26S proteasome subunit RPN8. RBSDV accumulation in L. striatellus increased after the 26S proteasome was disrupted by silencing the RPN8 expression. This finding indicated that L. striatellus 26S proteasome played a defense role against RBSDV infection by regulating RBSDV accumulation. Further investigations revealed that P9-1 could competitively bind to RPN8 with RPN7, thereby disrupting the assembly of 26S proteasome in L. striatellus and promoting the infection of RBSDV in insect vectors, and further affecting the transmission of the virus to rice by insect vectors. Similar to P9-1, rice stripe virus (RSV) NS2, a weak silencing suppressor, regulated virus accumulation and transmission by hijacking RPN8 to interfere with the function of 26S proteasome in L. striatellus.CONCLUSION: These results suggest that viruses promote their own infection via interfering with ubiquitination pathway of insect vectors, and this mechanism might be of universal importance. These findings provide a new insight into the mechanism of virus transmission in insect vectors.

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CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis

Abstract: CEPR2 interacts with some PYLs to promote their phosphorylation and degradation, whereas ABA inhibits this process. Thus, CEPR2 balances the growth regulation and stress response in Arabidopsis.

Cited by 74 publications

References 49 publications

The stability and ABA import activity of NRT1.2 inArabidopsisare regulated by CEPR2 via phosphorylation modification

The stability and ABA import activity of NRT1.2 inArabidopsisare regulated by CEPR2 via phosphorylation modification

Abscisic Acid Regulates Fleshy Fruit Ripening and Stress Resistance

Silencing suppressors of rice black‐streaked dwarf virus and rice stripe virus hijack the 26S proteasome of Laodelphax striatellus to facilitate virus accumulation and transmission

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