4.8 Article

Gibberellin-mediated proteasome-dependent degradation of the barley DELLA protein SLN1 repressor

Journal

PLANT CELL
Volume 14, Issue 12, Pages 3191-3200

Publisher

AMER SOC PLANT BIOLOGISTS
DOI: 10.1105/tpc.006197

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Funding

  1. Biotechnology and Biological Sciences Research Council [BBS/E/J/00000583] Funding Source: researchfish
  2. Biotechnology and Biological Sciences Research Council [BBS/E/J/00000583] Funding Source: Medline

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DELLA proteins are nuclear repressors of plant gibberellin (GA) responses. Here, we investigate the properties of SLN1, a DELLA protein from barley that is destabilized by GA treatment. Using specific inhibitors of proteasome function, we show that proteasome-mediated protein degradation is necessary for GA-mediated destabilization of SLN1. We also show that GA responses, such as the aleurone alpha-amylase response and seedling leaf extension growth, require proteasome-dependent GA-mediated SLN1 destabilization. In further experiments with protein kinase and protein phosphatase inhibitors, we identify two additional signaling steps that are necessary for GA response and for GA-mediated destabilization of SLN1. Thus, GA signaling involves protein phosphorylation and dephosphorylation steps and promotes the derepression of GA responses via proteasome-dependent destabilization of DELLA repressors.

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