ReseaRch highlights

SIGNALLING

ABAs greatest hits

Abscisic acid (ABA) is a ubiquitous plant hormone that regulates various aspects of plant growth and development, including seed maturation and dormancy, and has a central role in the adaptation of vegetative tissues to environmental stresses, notably drought. Although many components of the ABA signalling pathway are known, the identity and signalling mechanisms of ABA receptors have remained elusive. Now, six research groups report the mechanism by which the pyrabactin resistance (PYR)/PYR-like (PYL)/regulatory component of ABA receptors (RCAR) family of START proteins, previously identified as ABA receptors, bind ABA and positively regulate ABA signalling. Previous findings have reported that the Arabidopsis thaliana PYR/ PYL/RCAR proteins function as ABA receptors that, following ABA binding, inhibit the activity of known negative regulators of ABA signalling the type 2C protein phosphatases (PP2Cs) ABI1, ABI2, HAB1, HAB2 and PP2CA in both seeds and vegetative tissues. The suggested model predicts that, in the presence of ABA, PYR/PYL/RCARs bind to PP2Cs and induce the release of SNRK2 Ser/Thr kinases from PP2Cs, which would otherwise keep SNRK2s in an inactive state. SNRK2s can then phosphorylate downstream substrates, including ABA responsive element-binding protein (AREB) and ABA responsive element-binding factor (ABF) bZIP transcription factors, which activate ABA-responsive genes and ABA-related responses. In vitro studies by Fujii et al. show that combining PYR1, ABI1, SNRK2.6 (also known as SRK2E) and ABF2 is sufficient for ABAtriggered ABF2 phosphorylation. This indicates that these four proteins are the core components of the ABA signalling pathway. The other five groups carried out structural analyses of PYL1, PYL2, PYR1 and PYR2 alone, bound to

ABA or in complex with both ABA and PP2Cs. The data reveal how ABA binding induces a conformational change that allows the receptors to stably bind to PP2Cs. PYR and PYL have a seven-stranded curved -sheet that forms a central cavity resembling that of a folded hand. The surface of the cavity also comprises -helices, which, together with the inner side of the -sheet, constitute the ABA-binding site. Two highly conserved -loops act as cavity lids, which, in the absence of ABA, are in an open conformation that allows ABA to access the cavity. On ABA binding, the -loops adopt a closed-lid conformation. Importantly, this conformational change modifies the lid to create a binding site for PP2C. The receptorPP2C interaction results in the -loops covering the PP2C active site, thereby inhibiting its activity. This suggests that ABA receptors function as PP2C inhibitors in an ABA-dependent manner. Understanding the structural basis of ABA receptor interactions has important implications as it paves the way for the design of agonist molecules that could increase the resistance of crops to water stress.
ORIGINAL RESEARCH PAPERS Fujii, H. et al. In vitro reconstitution of an abscisic acid signalling pathway. Nature 462, 660664 (2009) | Nishimura, N. et al. Structural mechanism of abscisic acid binding and signaling by dimeric PYR1. Science 326, 13731379 (2009) | Miyazono, K. et al. Structural basis of abscisic acid signalling. Nature 462, 609614 (2009) | Melcher, K. et al. A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature 462, 602608 (2009) | Santiago, J. et al. The abscisic acid receptor PYR1 in complex with abscisic acid. Nature 462, 665668 (2009) | Yin, P. et al. Structural insights into the mechanism of abscisic acid signaling by PYL proteins. Nature Struct. Mol. Biol. 16, 12301236 (2009)

STOCKBYTE

Kim Baumann

ABA receptors function as PP2C inhibitors in an ABAdependent manner.

NATURE REvIEwS | MoleculAr cell Biology 2009 Macmillan Publishers Limited. All rights reserved

vOLUmE 11 | jANUARY 2010