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A thermodynamic switch modulates abscisic acid receptor sensitivity
Author(s) -
Dupeux Florine,
Santiago Julia,
Betz Katja,
Twycross Jamie,
Park SangYoul,
Rodriguez Lesia,
GonzalezGuzman Miguel,
Jensen Malene Ringkjøbing,
Krasnogor Natalio,
Blackledge Martin,
Holdsworth Michael,
Cutler Sean R,
Rodriguez Pedro L,
Márquez José Antonio
Publication year - 2011
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2011.294
Subject(s) - biology , abscisic acid , sensitivity (control systems) , receptor , biophysics , microbiology and biotechnology , biochemistry , gene , electronic engineering , engineering
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.