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

Open access
He, Jun-Xian, Gendron, Joshua M., Yang, Yanli, Li, Jianming, Wang, Zhi-Yong·2002·Proceedings of the National Academy of Sciences

Abstract

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 in vitro , and negatively regulates BZR1 protein accumulation in vivo . 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.

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Metadata

Authors
He, J.-X., Gendron, J. M., Yang, Y., Li, J., & Wang, Z.-Y.
Venue
Proceedings of the National Academy of Sciences
Published
2002-07-11
Volume
99
Issue
15
Pages
10185-10190
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2061619931
Cited by
717
References
2
FWCI
28.21
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis. https://app.cochat.ai/papers/10.1073/pnas.152342599
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He, J.-X., Gendron, J. M., Yang, Y., Li, J., & Wang, Z.-Y. (2002). The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.152342599

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