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CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis
Pyrabactin resistance 1 (PYR1)/PYR1-like (PYL) abscisic acid (ABA) receptors have been proved to be recruited in the plasma membrane (PM). In order to explain the roles of PYR/PYLs in the PM, PYL4 was used as bait to screen the PM-localized leucine-rich repeat receptor-like kinase family, and five m...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793440/ https://www.ncbi.nlm.nih.gov/pubmed/31232446 http://dx.doi.org/10.1093/jxb/erz302 |
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author | Yu, Zipeng Zhang, Di Xu, Yang Jin, Songsong Zhang, Lei Zhang, Shizhong Yang, Guodong Huang, Jinguang Yan, Kang Wu, Changai Zheng, Chengchao |
author_facet | Yu, Zipeng Zhang, Di Xu, Yang Jin, Songsong Zhang, Lei Zhang, Shizhong Yang, Guodong Huang, Jinguang Yan, Kang Wu, Changai Zheng, Chengchao |
author_sort | Yu, Zipeng |
collection | PubMed |
description | Pyrabactin resistance 1 (PYR1)/PYR1-like (PYL) abscisic acid (ABA) receptors have been proved to be recruited in the plasma membrane (PM). In order to explain the roles of PYR/PYLs in the PM, PYL4 was used as bait to screen the PM-localized leucine-rich repeat receptor-like kinase family, and five members were found directly interacting with PYL4. Loss of function by T-DNA insertion in C-terminally encoded peptide receptor 2 (CEPR2) together with phloem intercalated with xylem (PXY) and PXY-Like 2 (PXL2) led to ABA hypersensitivity, while CEPR2 overexpression led to ABA insensitivity compared with the wild type, indicating the redundant and negative roles of CEPR2, PXY, and PXL2 in ABA signaling. The PYL4 proteins were strongly accumulated in cepr2/pxy/pxl2 compared with the wild type. Furthermore, higher phosphorylation levels accompanied by lower protein levels of PYL4 in CEPR2 overexpression lines were observed, indicating the requirement of phosphorylation of PYLs for degradation. Subsequently, MS and in vitro kinase assays demonstrated that CEPR2 phosphorylated PYL4 at Ser54, while this phosphorylation was diminished or even eliminated in the presence of ABA. Taken together, CEPR2 promotes the phosphorylation and degradation of PYLs in unstressed conditions, whereas ABA represses this process to initiate ABA response during times of stress. |
format | Online Article Text |
id | pubmed-6793440 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-67934402019-10-18 CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis Yu, Zipeng Zhang, Di Xu, Yang Jin, Songsong Zhang, Lei Zhang, Shizhong Yang, Guodong Huang, Jinguang Yan, Kang Wu, Changai Zheng, Chengchao J Exp Bot Research Papers Pyrabactin resistance 1 (PYR1)/PYR1-like (PYL) abscisic acid (ABA) receptors have been proved to be recruited in the plasma membrane (PM). In order to explain the roles of PYR/PYLs in the PM, PYL4 was used as bait to screen the PM-localized leucine-rich repeat receptor-like kinase family, and five members were found directly interacting with PYL4. Loss of function by T-DNA insertion in C-terminally encoded peptide receptor 2 (CEPR2) together with phloem intercalated with xylem (PXY) and PXY-Like 2 (PXL2) led to ABA hypersensitivity, while CEPR2 overexpression led to ABA insensitivity compared with the wild type, indicating the redundant and negative roles of CEPR2, PXY, and PXL2 in ABA signaling. The PYL4 proteins were strongly accumulated in cepr2/pxy/pxl2 compared with the wild type. Furthermore, higher phosphorylation levels accompanied by lower protein levels of PYL4 in CEPR2 overexpression lines were observed, indicating the requirement of phosphorylation of PYLs for degradation. Subsequently, MS and in vitro kinase assays demonstrated that CEPR2 phosphorylated PYL4 at Ser54, while this phosphorylation was diminished or even eliminated in the presence of ABA. Taken together, CEPR2 promotes the phosphorylation and degradation of PYLs in unstressed conditions, whereas ABA represses this process to initiate ABA response during times of stress. Oxford University Press 2019-10-01 2019-06-21 /pmc/articles/PMC6793440/ /pubmed/31232446 http://dx.doi.org/10.1093/jxb/erz302 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Papers Yu, Zipeng Zhang, Di Xu, Yang Jin, Songsong Zhang, Lei Zhang, Shizhong Yang, Guodong Huang, Jinguang Yan, Kang Wu, Changai Zheng, Chengchao CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title | CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title_full | CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title_fullStr | CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title_full_unstemmed | CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title_short | CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis |
title_sort | cepr2 phosphorylates and accelerates the degradation of pyr/pyls in arabidopsis |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793440/ https://www.ncbi.nlm.nih.gov/pubmed/31232446 http://dx.doi.org/10.1093/jxb/erz302 |
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