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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
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    References listed on IDEAS

    as
    1. 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.
    2. 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.
    3. 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.
    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.
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    Cited by:

    1. Justine K. Kitony & Kelly Colt & Bradley W. Abramson & Nolan T. Hartwick & Semar Petrus & Emadeldin H. E. Konozy & Nisa Karimi & Levi Yant & Todd P. Michael, 2024. "Chromosome-level baobab genome illuminates its evolutionary trajectory and environmental adaptation," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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