IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-45575-7.html
   My bibliography  Save this article

Phosphorylation of Arabidopsis UVR8 photoreceptor modulates protein interactions and responses to UV-B radiation

Author

Listed:
  • Wei Liu

    (University of Glasgow)

  • Giovanni Giuriani

    (University of Glasgow)

  • Anezka Havlikova

    (University of Glasgow)

  • Dezhi Li

    (University of Glasgow)

  • Douglas J. Lamont

    (University of Dundee)

  • Susanne Neugart

    (Georg-August-Universität Göttingen)

  • Christos N. Velanis

    (University of Glasgow
    The Open University, Walton Hall Campus)

  • Jan Petersen

    (University of Glasgow
    Friedrich Schiller University)

  • Ute Hoecker

    (University of Köln)

  • John M. Christie

    (University of Glasgow)

  • Gareth I. Jenkins

    (University of Glasgow)

Abstract

Exposure of plants to ultraviolet-B (UV-B) radiation initiates transcriptional responses that modify metabolism, physiology and development to enhance viability in sunlight. Many of these regulatory responses to UV-B radiation are mediated by the photoreceptor UV RESISTANCE LOCUS 8 (UVR8). Following photoreception, UVR8 interacts directly with multiple proteins to regulate gene expression, but the mechanisms that control differential protein binding to initiate distinct responses are unknown. Here we show that UVR8 is phosphorylated at several sites and that UV-B stimulates phosphorylation at Serine 402. Site-directed mutagenesis to mimic Serine 402 phosphorylation promotes binding of UVR8 to REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins, which negatively regulate UVR8 action. Complementation of the uvr8 mutant with phosphonull or phosphomimetic variants suggests that phosphorylation of Serine 402 modifies UVR8 activity and promotes flavonoid biosynthesis, a key UV-B-stimulated response that enhances plant protection and crop nutritional quality. This research provides a basis to understand how UVR8 interacts differentially with effector proteins to regulate plant responses to UV-B radiation.

Suggested Citation

  • Wei Liu & Giovanni Giuriani & Anezka Havlikova & Dezhi Li & Douglas J. Lamont & Susanne Neugart & Christos N. Velanis & Jan Petersen & Ute Hoecker & John M. Christie & Gareth I. Jenkins, 2024. "Phosphorylation of Arabidopsis UVR8 photoreceptor modulates protein interactions and responses to UV-B radiation," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45575-7
    DOI: 10.1038/s41467-024-45575-7
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-45575-7
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-024-45575-7?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Di Wu & Qi Hu & Zhen Yan & Wen Chen & Chuangye Yan & Xi Huang & Jing Zhang & Panyu Yang & Haiteng Deng & Jiawei Wang & XingWang Deng & Yigong Shi, 2012. "Structural basis of ultraviolet-B perception by UVR8," Nature, Nature, vol. 484(7393), pages 214-219, April.
    2. Xiankun Li & Zheyun Liu & Haisheng Ren & Mainak Kundu & Frank W. Zhong & Lijuan Wang & Jiali Gao & Dongping Zhong, 2022. "Dynamics and mechanism of dimer dissociation of photoreceptor UVR8," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    3. Inyup Paik & Fulu Chen & Vinh Ngoc Pham & Ling Zhu & Jeong-Il Kim & Enamul Huq, 2019. "A phyB-PIF1-SPA1 kinase regulatory complex promotes photomorphogenesis in Arabidopsis," Nature Communications, Nature, vol. 10(1), pages 1-17, December.
    4. Ashutosh Sharma & Bhavana Sharma & Scott Hayes & Konstantin Kerner & Ute Hoecker & Gareth I. Jenkins & Keara A. Franklin, 2019. "UVR8 disrupts stabilisation of PIF5 by COP1 to inhibit plant stem elongation in sunlight," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Ruth Jean Ae Kim & De Fan & Jiangman He & Keunhwa Kim & Juan Du & Meng Chen, 2024. "Photobody formation spatially segregates two opposing phytochrome B signaling actions of PIF5 degradation and stabilization," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Hui-Hsien Chang & Lin-Chen Huang & Karen S. Browning & Enamul Huq & Mei-Chun Cheng, 2024. "The phosphorylation of carboxyl-terminal eIF2α by SPA kinases contributes to enhanced translation efficiency during photomorphogenesis," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Shichen Li & Zhihui Sun & Qing Sang & Chao Qin & Lingping Kong & Xin Huang & Huan Liu & Tong Su & Haiyang Li & Milan He & Chao Fang & Lingshuang Wang & Shuangrong Liu & Bin Liu & Baohui Liu & Xiangdon, 2023. "Soybean reduced internode 1 determines internode length and improves grain yield at dense planting," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Shan Hu & Yihan Chen & Chongzhen Qian & Hui Ren & Xinwen Liang & Wenjing Tao & Yanling Chen & Jue Wang & Yuan Dong & Jiupan Han & Xinhao Ouyang & Xi Huang, 2024. "Nuclear accumulation of rice UV-B photoreceptors is UV-B- and OsCOP1-independent for UV-B responses," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    5. Seong Ok Kim & So Ri Yun & Hyosub Lee & Junbeom Jo & Doo-Sik Ahn & Doyeong Kim & Irina Kosheleva & Robert Henning & Jungmin Kim & Changin Kim & Seyoung You & Hanui Kim & Sang Jin Lee & Hyotcherl Ihee, 2024. "Serial X-ray liquidography: multi-dimensional assay framework for exploring biomolecular structural dynamics with microgram quantities," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45575-7. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.