Cryptochrome 1 promotes photomorphogenesis in Arabidopsis by displacing substrates from the COP1 ubiquitin ligase

IF 5.7 1区 生物学 Q1 PLANT SCIENCES The Plant Journal Pub Date : 2025-03-07 DOI:10.1111/tpj.70071
Laura Trimborn, Franziska Kuttig, Jathish Ponnu, Pengxin Yu, Kris R. Korsching, Patrick Lederer, Uriel Urquiza-García, Matias D. Zurbriggen, Ute Hoecker
{"title":"Cryptochrome 1 promotes photomorphogenesis in Arabidopsis by displacing substrates from the COP1 ubiquitin ligase","authors":"Laura Trimborn,&nbsp;Franziska Kuttig,&nbsp;Jathish Ponnu,&nbsp;Pengxin Yu,&nbsp;Kris R. Korsching,&nbsp;Patrick Lederer,&nbsp;Uriel Urquiza-García,&nbsp;Matias D. Zurbriggen,&nbsp;Ute Hoecker","doi":"10.1111/tpj.70071","DOIUrl":null,"url":null,"abstract":"<p>In blue light, cryptochrome photoreceptors inhibit the key repressor of light signaling, the COP1/SPA ubiquitin ligase, to promote photomorphogenic responses. This inhibition relies on the direct interaction between COP1 and cryptochromes. Here, we analyzed the molecular mechanism of CRY1-mediated inhibition of COP1. We show that the VP motif in the C-terminal domain of CRY1 is essential for the COP1-CRY1 interaction in Arabidopsis. Phenotypic analysis of transgenic Arabidopsis plants harboring a mutation in the VP motif reveals that the VP motif of CRY1 is required for blue light-induced responses, such as seedling de-etiolation and anthocyanin biosynthesis. Via its VP motif, CRY1 inhibits the interaction between COP1 and the COP1 substrate transcription factors PAP2 and HY5. Replacing the VP motif of CRY1 with that of the human COP1 interactor TRIB1 produces a functional photoreceptor in transgenic plants. Since HY5, PAP2 and CRY1 interact with COP1 through their respective VP motifs, our results demonstrate that CRY1 inhibits the activity of COP1 by competitively displacing substrates from COP1. Taken together with previous results showing VP-dependent substrate displacement by photoactivated CRY2 and UVR8 photoreceptors, our results highlight the conservation of this mechanism across multiple photoreceptors.</p>","PeriodicalId":233,"journal":{"name":"The Plant Journal","volume":"121 5","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/tpj.70071","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Plant Journal","FirstCategoryId":"2","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/tpj.70071","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

In blue light, cryptochrome photoreceptors inhibit the key repressor of light signaling, the COP1/SPA ubiquitin ligase, to promote photomorphogenic responses. This inhibition relies on the direct interaction between COP1 and cryptochromes. Here, we analyzed the molecular mechanism of CRY1-mediated inhibition of COP1. We show that the VP motif in the C-terminal domain of CRY1 is essential for the COP1-CRY1 interaction in Arabidopsis. Phenotypic analysis of transgenic Arabidopsis plants harboring a mutation in the VP motif reveals that the VP motif of CRY1 is required for blue light-induced responses, such as seedling de-etiolation and anthocyanin biosynthesis. Via its VP motif, CRY1 inhibits the interaction between COP1 and the COP1 substrate transcription factors PAP2 and HY5. Replacing the VP motif of CRY1 with that of the human COP1 interactor TRIB1 produces a functional photoreceptor in transgenic plants. Since HY5, PAP2 and CRY1 interact with COP1 through their respective VP motifs, our results demonstrate that CRY1 inhibits the activity of COP1 by competitively displacing substrates from COP1. Taken together with previous results showing VP-dependent substrate displacement by photoactivated CRY2 and UVR8 photoreceptors, our results highlight the conservation of this mechanism across multiple photoreceptors.

Abstract Image

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
隐色素1通过取代COP1泛素连接酶的底物促进拟南芥的光形态形成
在蓝光下,隐色素光感受器抑制光信号的关键抑制因子COP1/SPA泛素连接酶,从而促进光形态形成反应。这种抑制依赖于COP1和隐色素之间的直接相互作用。在这里,我们分析了cry1介导的COP1抑制的分子机制。我们发现在拟南芥中,CRY1 c端结构域的VP基序对于COP1-CRY1相互作用至关重要。对含有VP基序突变的转基因拟南芥植株的表型分析表明,CRY1的VP基序在蓝光诱导的反应中是必需的,如幼苗去黄化和花青素的生物合成。CRY1通过VP基序抑制COP1与COP1底物转录因子PAP2和HY5之间的相互作用。用人类COP1相互作用物TRIB1取代CRY1的VP基序,在转基因植物中产生功能性光感受器。由于HY5、PAP2和CRY1通过各自的VP基序与COP1相互作用,我们的研究结果表明,CRY1通过竞争性地取代COP1的底物来抑制COP1的活性。结合先前的结果显示,光激活的CRY2和UVR8光感受器引起了vp依赖的底物位移,我们的结果强调了这种机制在多个光感受器中的守恒性。
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
The Plant Journal
The Plant Journal 生物-植物科学
CiteScore
13.10
自引率
4.20%
发文量
415
审稿时长
2.3 months
期刊介绍: Publishing the best original research papers in all key areas of modern plant biology from the world"s leading laboratories, The Plant Journal provides a dynamic forum for this ever growing international research community. Plant science research is now at the forefront of research in the biological sciences, with breakthroughs in our understanding of fundamental processes in plants matching those in other organisms. The impact of molecular genetics and the availability of model and crop species can be seen in all aspects of plant biology. For publication in The Plant Journal the research must provide a highly significant new contribution to our understanding of plants and be of general interest to the plant science community.
期刊最新文献
The C2 domain-containing and Ca2+-binding protein OsERG1 interferes with OsPYL10-OsPP2C09 module to negatively regulate the chilling tolerance in rice. OsCLSY4 modulates epigenomic patterns and grain size in rice. IMB4 integrates into brassinosteroid signaling to regulate hypocotyl growth. A major latex protein, TaSTP, coordinates sugar-antioxidant synergy to enhance drought tolerance in wheat. The trans-Golgi network adaptor protein 4 complex contributes to basal defense and immunity mediated through plasma membrane and intracellular immune receptors.
×
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:604180095
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