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CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1

Author

Listed:
  • Ling Zhu

    (The University of Texas at Austin)

  • Qingyun Bu

    (The University of Texas at Austin
    Present address: Northeast Institute of Geography and Agroecology, Chinese Academy of Sciences, Harbin 150081, China)

  • Xiaosa Xu

    (The University of Texas at Austin)

  • Inyup Paik

    (The University of Texas at Austin)

  • Xi Huang

    (Peking–Yale Joint Center for Plant Molecular Genetics and Agro-Biotechnology, State Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University
    Present address: School of Life Sciences, Xiamen University, Xiamen 361102, China)

  • Ute Hoecker

    (Botanical Institute and Cluster of Excellence on Plant Sciences (CEPLAS), Biocenter, University of Cologne)

  • Xing Wang Deng

    (Peking–Yale Joint Center for Plant Molecular Genetics and Agro-Biotechnology, State Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University)

  • Enamul Huq

    (The University of Texas at Austin)

Abstract

Plants undergo contrasting developmental programs in dark and light. Photomorphogenesis, a light-adapted programme is repressed in the dark by the synergistic actions of CUL4COP1–SPA E3 ubiquitin ligase and a subset of basic helix-loop-helix transcription factors called phytochrome interacting factors (PIFs). To promote photomorphogenesis, light activates the phytochrome family of sensory photoreceptors, which inhibits these repressors by poorly understood mechanisms. Here, we show that the CUL4COP1–SPA E3 ubiquitin ligase is necessary for the light-induced degradation of PIF1 in Arabidopsis. The light-induced ubiquitylation and subsequent degradation of PIF1 is reduced in the cop1, spaQ and cul4 backgrounds. COP1, SPA1 and CUL4 preferentially form complexes with the phosphorylated forms of PIF1 in response to light. The cop1 and spaQ seeds display strong hyposensitive response to far-red light-mediated seed germination and light-regulated gene expression. These data show a mechanism by which an E3 ligase attenuates its activity by degrading its cofactor in response to light.

Suggested Citation

  • Ling Zhu & Qingyun Bu & Xiaosa Xu & Inyup Paik & Xi Huang & Ute Hoecker & Xing Wang Deng & Enamul Huq, 2015. "CUL4 forms an E3 ligase with COP1 and SPA to promote light-induced degradation of PIF1," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8245
    DOI: 10.1038/ncomms8245
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    Cited by:

    1. 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.
    2. 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.
    3. Giorgia Capasso & Giorgia Santini & Mariagioia Petraretti & Sergio Esposito & Simone Landi, 2021. "Wild and Traditional Barley Genomic Resources as a Tool for Abiotic Stress Tolerance and Biotic Relations," Agriculture, MDPI, vol. 11(11), pages 1-15, November.

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