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A phyB-PIF1-SPA1 kinase regulatory complex promotes photomorphogenesis in Arabidopsis

Author

Listed:
  • Inyup Paik

    (The University of Texas at Austin)

  • Fulu Chen

    (The University of Texas at Austin
    Institute of Crop Sciences, Chinese Academy of Agricultural Sciences)

  • Vinh Ngoc Pham

    (The University of Texas at Austin)

  • Ling Zhu

    (The University of Texas at Austin
    Syngenta Crop Protection, LLC.)

  • Jeong-Il Kim

    (The University of Texas at Austin
    Chonnam National University)

  • Enamul Huq

    (The University of Texas at Austin)

Abstract

CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1) is a highly conserved E3 ubiquitin ligase from plants to animals and acts as a central repressor of photomorphogenesis in plants. SUPPRESSOR OF PHYA-105 1 family members (SPA1-SPA4) directly interact with COP1 and enhance COP1 activity. Despite the presence of a kinase domain at the N-terminus, no COP1-independent role of SPA proteins has been reported. Here we show that SPA1 acts as a serine/threonine kinase and directly phosphorylates PIF1 in vitro and in vivo. SPAs are necessary for the light-induced phosphorylation, ubiquitination and subsequent degradation of PIF1. Moreover, the red/far-red light photoreceptor phyB interacts with SPA1 through its C-terminus and enhances the recruitment of PIF1 for phosphorylation. These data provide a mechanistic view on how the COP1-SPA complexes serve as an example of a cognate kinase-E3 ligase complex that selectively triggers rapid phosphorylation and removal of its substrates, and how phyB modulates this process to promote photomorphogenesis.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12110-y
    DOI: 10.1038/s41467-019-12110-y
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    Cited by:

    1. 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.
    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. 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.

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