COP1 destabilizes DELLA proteins inArabidopsis

Author:

Blanco-Touriñán Noel,Legris Martina,Minguet Eugenio G.,Costigliolo-Rojas Cecilia,Nohales María A.,Iniesto Elisa,García-León Marta,Pacín Manuel,Heucken Nicole,Blomeier Tim,Locascio Antonella,Černý Martin,Esteve-Bruna David,Díez-Díaz Mónica,Brzobohatý Břetislav,Frerigmann Henning,Zurbriggen Matías D.,Kay Steve A.,Rubio Vicente,Blázquez Miguel A.,Casal Jorge J.,Alabadí DavidORCID

Abstract

AbstractDELLA transcriptional regulators are central components in the control of plant body form in response to the environment. This is considered to be mediated by changes in the metabolism of the hormones gibberellins (GAs), which promote the degradation of DELLAs. However, here we show that warm temperature or shade reduced the stability of a GA-insensitive DELLA allele inArabidopsis. Furthermore, the degradation of DELLA induced by the warmth anticipated changes in GA levels and depended on the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1). COP1 enhanced the degradation of normal and GA-insensitive DELLA alleles when co-expressed inN. benthamiana.DELLA proteins physically interacted with COP1 in yeast, mammalian and plant cells. This interaction was enhanced by the COP1 complex partner SUPRESSOR OFphyA-1051 (SPA1). The level of ubiquitination of DELLA was enhanced by COP1 and COP1 ubiquitinated DELLA proteins in vitro. We propose that DELLAs are destabilized not only by the canonical GA-dependent pathway but also by COP1 and that this control is relevant for growth responses to shade and warm temperature.SignificanceDELLA proteins are plant-specific transcriptional regulators that act as signaling hubs at the interface between the environment and the transcriptional networks that control growth. DELLAs are destabilized by the growth-promoting hormone gibberellin, whose levels are very sensitive to environmental changes. Here we describe an alternative pathway to destabilize these proteins. We show that DELLAs are substrate of COP1, an E3 ubiquitin ligase that increases its nuclear activity to promote growth in response to shade or warmth. Our results also show that the destabilization of DELLAs by COP1 precedes the action of gibberellins, suggesting the existence of a sequential mechanism to control the stability of these proteins.

Publisher

Cold Spring Harbor Laboratory

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