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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Aprotinin / pharmacology
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Cysteine Endopeptidases / metabolism*
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Enzyme Induction / drug effects
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Enzyme Inhibitors / pharmacology
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Gibberellins / pharmacology*
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Hordeum / drug effects
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Hordeum / genetics*
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Hordeum / growth & development
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Multienzyme Complexes / metabolism*
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Mutation
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Okadaic Acid / pharmacology
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Phenylmethylsulfonyl Fluoride / pharmacology
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Plant Leaves / drug effects
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Plant Leaves / genetics
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Plant Leaves / growth & development
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Plant Proteins / drug effects
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Plant Proteins / genetics*
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Plant Proteins / metabolism
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Proteasome Endopeptidase Complex
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Seeds / drug effects
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Seeds / genetics
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Seeds / metabolism
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Signal Transduction
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Sulfones / pharmacology
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Vanadates / pharmacology
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alpha-Amylases / biosynthesis
Substances
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Enzyme Inhibitors
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Gibberellins
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Multienzyme Complexes
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Plant Proteins
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Sulfones
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Okadaic Acid
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4-(2-aminoethyl)benzenesulfonylfluoride
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Vanadates
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Phenylmethylsulfonyl Fluoride
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Aprotinin
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alpha-Amylases
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex