C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 contributes to GA-mediated growth and flowering by interaction with DELLA proteins

IF 8.3 1区 生物学 Q1 PLANT SCIENCES New Phytologist Pub Date : 2024-04-09 DOI:10.1111/nph.19742
Ting Li, Yongqin Wang, Annelore Natran, Yi Zhang, Hao Wang, Kangxi Du, Peng Qin, Hua Yuan, Weilan Chen, Bin Tu, Dirk Inzé, Marieke Dubois
{"title":"C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 contributes to GA-mediated growth and flowering by interaction with DELLA proteins","authors":"Ting Li,&nbsp;Yongqin Wang,&nbsp;Annelore Natran,&nbsp;Yi Zhang,&nbsp;Hao Wang,&nbsp;Kangxi Du,&nbsp;Peng Qin,&nbsp;Hua Yuan,&nbsp;Weilan Chen,&nbsp;Bin Tu,&nbsp;Dirk Inzé,&nbsp;Marieke Dubois","doi":"10.1111/nph.19742","DOIUrl":null,"url":null,"abstract":"<div>\n \n <p>\n </p><ul>\n \n <li>Gibberellic acid (GA) plays a central role in many plant developmental processes and is crucial for crop improvement. DELLA proteins, the core suppressors in the GA signaling pathway, are degraded by GA via the 26S proteasomal pathway to release the GA response. However, little is known about the phosphorylation-mediated regulation of DELLA proteins.</li>\n \n <li>In this study, we combined GA response assays with protein–protein interaction analysis to infer the connection between <i>Arabidopsis thaliana</i> DELLAs and the C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 (CPL3), a phosphatase involved in the dephosphorylation of RNA polymerase II.</li>\n \n <li>We show that CPL3 directly interacts with DELLA proteins and promotes DELLA protein stability by inhibiting its degradation by the 26S proteasome. Consequently, CPL3 negatively modulates multiple GA-mediated processes of plant development, including hypocotyl elongation, flowering time, and anthocyanin accumulation.</li>\n \n <li>Taken together, our findings demonstrate that CPL3 serves as a novel regulator that could improve DELLA stability and thereby participate in GA signaling transduction.</li>\n </ul>\n </div>","PeriodicalId":214,"journal":{"name":"New Phytologist","volume":"242 6","pages":"2555-2569"},"PeriodicalIF":8.3000,"publicationDate":"2024-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"New Phytologist","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/nph.19742","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
引用次数: 0

Abstract

  • Gibberellic acid (GA) plays a central role in many plant developmental processes and is crucial for crop improvement. DELLA proteins, the core suppressors in the GA signaling pathway, are degraded by GA via the 26S proteasomal pathway to release the GA response. However, little is known about the phosphorylation-mediated regulation of DELLA proteins.
  • In this study, we combined GA response assays with protein–protein interaction analysis to infer the connection between Arabidopsis thaliana DELLAs and the C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 (CPL3), a phosphatase involved in the dephosphorylation of RNA polymerase II.
  • We show that CPL3 directly interacts with DELLA proteins and promotes DELLA protein stability by inhibiting its degradation by the 26S proteasome. Consequently, CPL3 negatively modulates multiple GA-mediated processes of plant development, including hypocotyl elongation, flowering time, and anthocyanin accumulation.
  • Taken together, our findings demonstrate that CPL3 serves as a novel regulator that could improve DELLA stability and thereby participate in GA signaling transduction.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 通过与 DELLA 蛋白相互作用,为 GA 介导的生长和开花做出贡献
摘要 赤霉素(GA)在许多植物发育过程中起着核心作用,对作物改良至关重要。DELLA蛋白是GA信号通路中的核心抑制因子,可通过26S蛋白酶体途径被GA降解,从而释放GA反应。然而,人们对磷酸化介导的 DELLA 蛋白调控知之甚少。在这项研究中,我们结合了 GA 响应测定和蛋白-蛋白相互作用分析,推断拟南芥 DELLA 与 C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3(CPL3)之间的联系,C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 是一种参与 RNA 聚合酶 II 去磷酸化的磷酸酶。我们的研究表明,CPL3 直接与 DELLA 蛋白相互作用,并通过抑制 26S 蛋白酶体的降解来促进 DELLA 蛋白的稳定性。因此,CPL3 对植物发育过程中由 GA 介导的多个过程(包括下胚轴伸长、开花时间和花青素积累)具有负向调节作用。综上所述,我们的研究结果表明 CPL3 是一种新型调控因子,可提高 DELLA 的稳定性,从而参与 GA 信号转导。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
New Phytologist
New Phytologist 生物-植物科学
自引率
5.30%
发文量
728
期刊介绍: New Phytologist is an international electronic journal published 24 times a year. It is owned by the New Phytologist Foundation, a non-profit-making charitable organization dedicated to promoting plant science. The journal publishes excellent, novel, rigorous, and timely research and scholarship in plant science and its applications. The articles cover topics in five sections: Physiology & Development, Environment, Interaction, Evolution, and Transformative Plant Biotechnology. These sections encompass intracellular processes, global environmental change, and encourage cross-disciplinary approaches. The journal recognizes the use of techniques from molecular and cell biology, functional genomics, modeling, and system-based approaches in plant science. Abstracting and Indexing Information for New Phytologist includes Academic Search, AgBiotech News & Information, Agroforestry Abstracts, Biochemistry & Biophysics Citation Index, Botanical Pesticides, CAB Abstracts®, Environment Index, Global Health, and Plant Breeding Abstracts, and others.
期刊最新文献
Breaking into nature's secret medicine cabinet: lichens – a biochemical goldmine ready for discovery LATERAL FLORET 2 encoding a sucrose non-fermenting 2 chromatin remodeling factor regulates axillary meristem of spikelet development in rice (Oryza sativa) A transposon-based cargo system mediates gene trafficking and creates ultra-clean transgenic plants after stable transformation The airborne herbivore-induced plant volatile indole is converted to benzoxazinoid defense compounds in maize plants A novel peptide encoded by a rice circular RNA confers broad-spectrum disease resistance in rice plants
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1