The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in <i>Arabidopsis</i>

DOI Web Site 被引用文献23件
  • Jun-Xian He
    Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305; Department of Biological Sciences, Stanford University, Stanford, CA 94305; and Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109
  • Joshua M. Gendron
    Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305; Department of Biological Sciences, Stanford University, Stanford, CA 94305; and Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109
  • Yanli Yang
    Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305; Department of Biological Sciences, Stanford University, Stanford, CA 94305; and Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109
  • Jianming Li
    Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305; Department of Biological Sciences, Stanford University, Stanford, CA 94305; and Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109
  • Zhi-Yong Wang
    Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305; Department of Biological Sciences, Stanford University, Stanford, CA 94305; and Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109

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<jats:p> Brassinosteroids (BRs) are a class of steroid hormones essential for normal growth and development in plants. BR signaling involves the cell-surface receptor BRI1, the glycogen synthase kinase-3-like kinase BIN2 as a negative regulator, and nuclear proteins BZR1 and BZR2/BES1 as positive regulators. The interactions among these components remain unclear. Here we report that BRs induce dephosphorylation and accumulation of BZR1 protein. Experiments using a proteasome inhibitor, MG132, suggest that phosphorylation of BZR1 increases its degradation by the proteasome machinery. BIN2 directly interacts with BZR1 in yeast two-hybrid assays, phosphorylates BZR1 <jats:italic>in</jats:italic> <jats:italic>vitro</jats:italic> , and negatively regulates BZR1 protein accumulation <jats:italic>in</jats:italic> <jats:italic>vivo</jats:italic> . These results strongly suggest that BIN2 phosphorylates BZR1 and targets it for degradation and that BR signaling causes BZR1 dephosphorylation and accumulation by inhibiting BIN2 activity. </jats:p>

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