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First published online November 20, 2002; 10.1105/tpc.006197

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The Plant Cell, Vol. 14, 3191-3200, December 2002, Copyright © 2002,
American Society of Plant Biologists

Gibberellin-Mediated Proteasome-Dependent Degradation of the Barley DELLA Protein SLN1 Repressor

Xiangdong Fu1,a, Donald E. Richards1,a, Tahar Ait-alia, Llewelyn W. Hynesa, Helen Oughamb, Jinrong Peng2,a and Nicholas P. Harberd3,a

a John Innes Centre, Colney Lane, Norwich NR4 7UJ, United Kingdom
b Institute of Grassland and Environmental Research, Plas Gogerddan, Aberystwyth, Ceredigion SY23 3EB, Wales, United Kingdom

3 To whom correspondence should be addressed. E-mail nicholas.harberd{at}bbsrc.ac.uk; fax 44-1603-450025

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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