A thermodynamic switch modulates abscisic acid receptor sensitivity.

Détails

ID Serval
serval:BIB_C3D746234282
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A thermodynamic switch modulates abscisic acid receptor sensitivity.
Périodique
The EMBO journal
Auteur⸱e⸱s
Dupeux F., Santiago J., Betz K., Twycross J., Park S.Y., Rodriguez L., Gonzalez-Guzman M., Jensen M.R., Krasnogor N., Blackledge M., Holdsworth M., Cutler S.R., Rodriguez P.L., Márquez J.A.
ISSN
1460-2075 (Electronic)
ISSN-L
0261-4189
Statut éditorial
Publié
Date de publication
16/08/2011
Peer-reviewed
Oui
Volume
30
Numéro
20
Pages
4171-4184
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Résumé
Abscisic acid (ABA) is a key hormone regulating plant growth, development and the response to biotic and abiotic stress. ABA binding to pyrabactin resistance (PYR)/PYR1-like (PYL)/Regulatory Component of Abscisic acid Receptor (RCAR) intracellular receptors promotes the formation of stable complexes with certain protein phosphatases type 2C (PP2Cs), leading to the activation of ABA signalling. The PYR/PYL/RCAR family contains 14 genes in Arabidopsis and is currently the largest plant hormone receptor family known; however, it is unclear what functional differentiation exists among receptors. Here, we identify two distinct classes of receptors, dimeric and monomeric, with different intrinsic affinities for ABA and whose differential properties are determined by the oligomeric state of their apo forms. Moreover, we find a residue in PYR1, H60, that is variable between family members and plays a key role in determining oligomeric state. In silico modelling of the ABA activation pathway reveals that monomeric receptors have a competitive advantage for binding to ABA and PP2Cs. This work illustrates how receptor oligomerization can modulate hormonal responses and more generally, the sensitivity of a ligand-dependent signalling system.
Mots-clé
Abscisic Acid/metabolism, Arabidopsis/metabolism, Arabidopsis Proteins/metabolism, Membrane Transport Proteins/metabolism, Models, Biological, Phosphoprotein Phosphatases/metabolism, Protein Binding, Protein Phosphatase 2C, Receptors, Cell Surface/metabolism, Thermodynamics
Pubmed
Web of science
Open Access
Oui
Création de la notice
10/01/2019 17:22
Dernière modification de la notice
23/02/2022 6:36
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