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OsMAPK6 phosphorylation and CLG1 ubiquitylation of GW6a non-additively enhance rice grain size through stabilization of the substrate

Author

Listed:
  • Chen Bai

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Gao-Jie Wang

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Xiao-Hui Feng

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Qiong Gao

    (Chinese Academy of Sciences
    China National Botanical Garden)

  • Wei-Qing Wang

    (Chinese Academy of Sciences
    China National Botanical Garden)

  • Ran Xu

    (Institute of Hainan University, Hainan Yazhou Bay Seed Laboratory
    Hainan University)

  • Su-Jie Guo

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Shao-Yan Shen

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Ming Ma

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Wen-Hui Lin

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Chun-Ming Liu

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences)

  • Yunhai Li

    (University of Chinese Academy of Sciences
    Chinese Academy of Sciences
    Chinese Academy of Sciences)

  • Xian-Jun Song

    (Chinese Academy of Sciences
    China National Botanical Garden
    University of Chinese Academy of Sciences
    Chinese Academy of Sciences)

Abstract

The chromatin modifier GRAIN WEIGHT 6a (GW6a) enhances rice grain size and yield. However, little is known about its gene network determining grain size. Here, we report that MITOGEN-ACTIVED PROTEIN KINASE 6 (OsMAPK6) and E3 ligase CHANG LI GENG 1 (CLG1) interact with and target GW6a for phosphorylation and ubiquitylation, respectively. Unexpectedly, however, in vitro and in vivo assays reveal that both of the two post-translational modifications stabilize GW6a. Furthermore, we uncover two major GW6a phosphorylation sites (serine142 and threonine186) targeted by OsMAPK6 serving an important role in modulating grain size. In addition, our genetic and molecular results suggest that the OsMAPK6-GW6a and CLG1-GW6a axes are crucial and operate in a non-additive manner to control grain size. Overall, our findings identify a previously unknown mechanism by which phosphorylation and ubiquitylation non-additively stabilize GW6a to enhance grain size, and reveal correlations and interactions of these posttranslational modifications during rice grain development.

Suggested Citation

  • Chen Bai & Gao-Jie Wang & Xiao-Hui Feng & Qiong Gao & Wei-Qing Wang & Ran Xu & Su-Jie Guo & Shao-Yan Shen & Ming Ma & Wen-Hui Lin & Chun-Ming Liu & Yunhai Li & Xian-Jun Song, 2024. "OsMAPK6 phosphorylation and CLG1 ubiquitylation of GW6a non-additively enhance rice grain size through stabilization of the substrate," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-48786-0
    DOI: 10.1038/s41467-024-48786-0
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    References listed on IDEAS

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    1. Xiyu Ma & Lucas A. N. Claus & Michelle E. Leslie & Kai Tao & Zhiping Wu & Jun Liu & Xiao Yu & Bo Li & Jinggeng Zhou & Daniel V. Savatin & Junmin Peng & Brett M. Tyler & Antje Heese & Eugenia Russinova, 2020. "Ligand-induced monoubiquitination of BIK1 regulates plant immunity," Nature, Nature, vol. 581(7807), pages 199-203, May.
    2. Takanori Kobayashi & Seiji Nagasaka & Takeshi Senoura & Reiko Nakanishi Itai & Hiromi Nakanishi & Naoko K. Nishizawa, 2013. "Iron-binding haemerythrin RING ubiquitin ligases regulate plant iron responses and accumulation," Nature Communications, Nature, vol. 4(1), pages 1-12, December.
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