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

Xiangdong Fu, Donald E Richards, Tahar Ait-Ali, Llewelyn W Hynes, Helen Ougham, Jinrong Peng, Nicholas P Harberd

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)3191-200
Number of pages10
JournalPlant Cell
Volume14
Issue number12
DOIs
Publication statusPublished - Dec 2002

Keywords

  • Alleles
  • Aprotinin
  • Cysteine Endopeptidases
  • Enzyme Induction
  • Enzyme Inhibitors
  • Gibberellins
  • Hordeum
  • Multienzyme Complexes
  • Mutation
  • Okadaic Acid
  • Phenylmethylsulfonyl Fluoride
  • Plant Leaves
  • Plant Proteins
  • Proteasome Endopeptidase Complex
  • Seeds
  • Signal Transduction
  • Sulfones
  • Vanadates
  • alpha-Amylases

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