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Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex

ABSTRACT: Phytohormone abscisic acid (ABA) regulates key aspects of plant development such as seed germination, as well as responses to important environmental stresses, including drought, salinity and cold temperatures. The ABA signaling pathway is tightly controlled by the ubiquitin proteasome system. CULLIN4-RING E3 ubiquitin ligases use the substrate receptor module COP10-DDB1-DET1-DDA1 (CDDD) to target PYL8, one of the ABA receptors of the PYR/PYL/RCAR (pyrabactin resistance/pyrabactin resistance-like/regulatory components of ABA) family. Therefore, CRL4-CDDD complexes are negative regulators of ABA-mediated stress responses. Conversely, ABA treatments attenuate PYL8 receptor degradation, although the precise molecular details of this mechanism remained unknown. Here, we show that ABA promotes the disruption of CRL4-CDDD complexes, leading to PYL8 stabilization. ABA-mediated CRL4-CDDD dissociation likely involves altered association between DDA1-containing complexes and the CSN, a master regulator of the assembly of cullin-based E3 ligases, including CRL4-CDDD. Indeed, treatments with CSN5i-3, an inhibitor of the CSN activity, suppressed the ABA effect on CRL4-CDDD assembly. Altogether, our findings indicate that ABA stabilizes PYL8 by altering the dynamics of the CRL4-CDDD-CSN complex association, unveiling a regulatory mechanism by which a plant hormone inhibits an E3 ubiquitin ligase to protect its own receptors from degradation.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell

SUBMITTER: Alberto Paradela

LAB HEAD: Vicente Rubio

PROVIDER: PXD055583 | Pride | 2024-09-11

REPOSITORIES: Pride

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			Action	DRS
	20200226_MartaGarcia_01.wiff.zip	Wiff
	20200226_MartaGarcia_02.wiff.zip	Wiff
	20200226_MartaGarcia_03.wiff.zip	Wiff
	20200226_MartaGarcia_04.wiff.zip	Wiff
	20200226_MartaGarcia_05.wiff.zip	Wiff

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Project description:Fruit ripening is a very important physiological process which gains relevance in crop species due to their economical and nutritional repercussions. During fruit ripening enormous metabolic changes occur in a genetically-controlled scenario affecting the physiology of most cell compartments. Peroxisomes are single-membrane bounded organelles present in all eukaryotes which display a noteworthy nitro-oxidative metabolism, and harbor catalase as one of the major antioxidant enzymes in cells. Quantitative proteomics analysis by isobaric tags for relative and absolute quantification (iTRAQ) was used to investigate the ripening process in sweet pepper (Capsicum annuum L.) fruits. Out of 2,574 quantified proteins, 692 were found to be significantly more abundant in immature green fruits compared to red ones, but 497 showed a lower expression as the ripening proceeded. Overall, about 50% of the detectable proteins were estimated to modify their expression due to the ripening process. Data obtained from the Gene Ontology algorithms (AgriGO platform) showed that from all the identified proteins, 46 (2%) were only predicted to have a peroxisomal origin, with a high number of them displaying up-expression tendency during ripening. Catalase was framed within the group which showed lower expression in ripe fruits, but this enzyme was also susceptible to undergo posttranslational modifications (PTMs) promoted by reactive nitrogen and oxygen species (RNS and ROS) through nitration, S-nitrosylation and oxidation events which provoked its inhibition. The biochemical characterization of catalase indicates that it has atypical native molecular mass (125-135 kDa), since it behaves as a homodimer, and isoelectric point of 7.4, which is higher than that of the majority of plant catalases reported so far. Taking together, these data suggest that ROS and RNS could be essential to modulate the role of catalase for the maintenance of basic cellular peroxisomal functions during pepper fruit ripening where nitro-oxidative stress occur.

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Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex

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