ArticleProceedings of the National Academy of Sciences of the United States of America2026
Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Drought limits crop productivity, and effective mitigation requires a mechanistic understanding of how abscisic acid (ABA) perception translates hormone levels into physiological responses. In seed plants, ABA is sensed by PYR/PYL/RCAR (PYR/PYL) receptors, which inhibit 2C protein phosphatases (PP2Cs), thereby releasing Snf1-related protein kinases and driving stomatal closure and stress-responsive transcription. Yet how receptor architecture evolved to tune ABA dependence and dynamic range remains unclear. Here, we combine structural biology, biochemistry, evolutionary analysis, and in planta assays across algal, bryophyte, and angiosperm receptors to uncover a minimal molecular code that governs ABA sensitivity and oligomeric state. We identify a five-residue signature: Three leucines in the ligand pocket stabilize the gate in a closed conformation, conferring ligand-independent PP2C inhibition (ancestral trait), while two interface residues toggle dimerization (Leu/Lys) versus monomerization (Cys/Ser), thereby setting ABA affinity. Structure-guided swaps reciprocally convert behaviors: Introducing the three leucines plus interface substitutions renders the ABA-dependent dimeric
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