SPINDLY mediates <i>O</i>-fucosylation of hundreds of proteins and sugar-dependent growth in Arabidopsis

  • Yang Bi
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Ruben Shrestha
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Zhenzhen Zhang
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Chuan-Chih Hsu
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Andres V Reyes
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Sumudu Karunadasa
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Peter R Baker
    Department of Pharmaceutical Chemistry, University of California at San Francisco , San Francisco, California 94143 , USA
  • Jason C Maynard
    Department of Pharmaceutical Chemistry, University of California at San Francisco , San Francisco, California 94143 , USA
  • Yang Liu
    ThermoFisher Scientific , San Jose, California 95134 , USA
  • Amirmansoor Hakimi
    ThermoFisher Scientific , San Jose, California 95134 , USA
  • Daniel Lopez-Ferrer
    ThermoFisher Scientific , San Jose, California 95134 , USA
  • Tahmid Hassan
    ThermoFisher Scientific , Somerset, New Jersey 08873 , USA
  • Robert J Chalkley
    Department of Pharmaceutical Chemistry, University of California at San Francisco , San Francisco, California 94143 , USA
  • Shou-Ling Xu
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA
  • Zhi-Yong Wang
    Department of Plant Biology, Carnegie Institution for Science , Stanford, California 94305 , USA

抄録

<jats:title>Abstract</jats:title> <jats:p>The recent discovery of SPINDLY (SPY)-catalyzed protein O-fucosylation revealed a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates the important roles of SPY in diverse developmental and physiological processes. However, the upstream signal controlling SPY activity and the downstream substrate proteins O-fucosylated by SPY remain largely unknown. Here, we demonstrated that SPY mediates sugar-dependent growth in Arabidopsis (Arabidopsis thaliana). We further identified hundreds of O-fucosylated proteins using lectin affinity chromatography followed by mass spectrometry. All the O-fucosylation events quantified in our proteomic analyses were undetectable or dramatically decreased in the spy mutants, and thus likely catalyzed by SPY. The O-fucosylome includes mostly nuclear and cytosolic proteins. Many O-fucosylated proteins function in essential cellular processes, phytohormone signaling, and developmental programs, consistent with the genetic functions of SPY. The O-fucosylome also includes many proteins modified by O-linked N-acetylglucosamine (O-GlcNAc) and by phosphorylation downstream of the target of rapamycin (TOR) kinase, revealing the convergence of these nutrient signaling pathways on key regulatory functions such as post-transcriptional/translational regulation and phytohormone responses. Our study identified numerous targets of SPY/O-fucosylation and potential nodes of crosstalk among sugar/nutrient signaling pathways, enabling future dissection of the signaling network that mediates sugar regulation of plant growth and development.</jats:p>

収録刊行物

  • The Plant Cell

    The Plant Cell 35 (5), 1318-1333, 2023-02-06

    Oxford University Press (OUP)

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