Identification and mechanism of ABA receptor antagonism

Melcher, Karsten; Xu, Yong; Ng, Ley Moy; Zhou, Xin; Soon, F.-F.; Chinnusamy, Viswanathan; Suino-Powell, Kelly; Kovach, Amanda; Tham, Fook S.; Cutler, Sean R.; Li, Jun; Yong, Eu-Leong; Zhu, Jian‐Kang; Xu, Hongjiao

doi:10.1038/nsmb.1887

Cited by 150 publications

(170 citation statements)

References 35 publications

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“…GST-tagged PYL1 (∼51 kD) and PYL2 (∼46 kD) were pulled down by His-tagged PYL13 (∼22 kD) in an ABAindependent manner ( Figure 5C). Previous structural and biochemical investigations demonstrated that several PYLs (such as PYR1, PYL1, PYL2, PYL3) form homodimers in solution and that the dimer formation is important in regulating ABA binding and PP2C interactions [5,8,11,27,28,36,37]. Our results suggest that PYL13 can form heterodimers with other PYLs.…”

Section: Pyl13 Interacts With and Antagonizes Other Pylsmentioning

confidence: 58%

“…Several of the PYLs have been shown to bind and inhibit clade A protein phosphatase type 2Cs (PP2Cs, comprising ABI1, ABI2, HAB1, HAB2, AHG1, PP2CA, HAI1, HAI2, and HAI3) in the presence of ABA [2-4, 6, 7]. Structural studies confirmed that the PYLs are ABA receptors and showed that the PP2Cs can function as coreceptors because they enhance the ABA-binding affinities of the PYLs [5,[8][9][10][11]. In Arabidopsis protoplasts, PYR1 and PYLs 1-12 could release ABI1 inhibition of ABA-dependent activation of RD29B-LUC expression by the SnRK2 protein kinases such as OST1/SnRK2.6 [4].…”

Section: Introductionmentioning

confidence: 86%

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The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

et al. 2013

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Proteins in the PYR/PYL/RCAR family (PYLs) are known as receptors for the phytohormone ABA. Upon ABA binding, PYL adopts a conformation that allows it to interact with and inhibit clade A protein phosphatase 2Cs (PP2Cs), which are known as the co-receptors for ABA. Inhibition of the PP2Cs then leads to the activation of the SnRK2 family protein kinases that phosphorylate and activate downstream effectors in ABA response pathways. The PYL family has 14 members in Arabidopsis, 13 of which have been demonstrated to function as ABA receptors. The function of PYL13, a divergent member of the family, has been enigmatic. We report here that PYL13 differs from the other PYLs in three key residues that affect ABA perception, and mutations in these three residues can convert PYL13 into a partially functional ABA receptor. Transgenic plants overexpressing PYL13 show increased ABA sensitivity in seed germination and postgermination seedling establishment as well as decreased stomatal conductance, increased water-use efficiency, accelerated stress-responsive gene expression, and enhanced drought resistance. pyl13 mutant plants are less sensitive to ABA inhibition of postgermination seedling establishment. PYL13 interacts with and inhibits some members of clade A PP2Cs (PP2CA in particular) in an ABA-independent manner. PYL13 also interacts with the other PYLs and antagonizes their function as ABA receptors. Our results show that PYL13 is not an ABA receptor but can modulate the ABA pathway by interacting with and inhibiting both the PYL receptors and the PP2C co-receptors.

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Section: Pyl13 Interacts With and Antagonizes Other Pylsmentioning

confidence: 58%

Section: Introductionmentioning

confidence: 86%

The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

et al. 2013

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“…Therefore, it qualifies as a hypermorphic mutation in the presence of ABA and a PYR/PYL receptor, although paradoxically, hab1 G246D as well as abi1 G180D and abi2 G168D proteins, have a lower specific activity as compared to wt in the absence of ABA. [20,21,22,38]. Additionally, these studies reveal that whereas pyrabactin is an ABA-agonist for some PYR/PYL/RCAR receptors, e.g.…”

Section: Abi1-1 G180d Abi2-1 G168d and Hab1 G246d Hypermorphic Enzymesmentioning

confidence: 82%

“…A high degree of structural similarity is evident from the superposition of the three structures (Fig. 2), however, recent works using the pyrabactin molecule reveal subtle differences among the receptor binding pockets with important functional consequences, since pyrabactin is an agonist of PYR1 and PYL1, whereas it is an antagonist of PYL2 [20,21,22]. Different experimental data indicate that these receptors exist as dimers in solution, however, the receptor-PP2C complexes have a 1:1 stoichiometry, implying that the receptor dimers have to dissociate before interacting with the PP2C [17,18,19].…”

Section: The Structure Of Pyr/pyl/rcar Receptorsmentioning

confidence: 97%

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Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs

et al. 2012

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Abscisic acid (ABA) plays an essential function in plant physiology since it is required for biotic and abiotic stress responses as well as control of plant growth and development. A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of specific protein phosphatases type-2C (PP2Cs) in an ABAdependent manner. The structural and functional mechanism by which ABA is perceived by these receptors and consequently leads to inhibition of the PP2Cs has been recently elucidated. The module PYR/PYL/RCAR-ABA-PP2C offers an elegant and unprecedented mechanism to control phosphorylation signaling cascades in a ligand-dependent manner. The knowledge of their three-dimensional structures paves the way to the design of ABA agonists able to modulate the plant stress response.

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Structural Biology of Salt and Drought Tolerance in Plants

Sánchez-Barrena

Martı́nez-Ripoll

Albert

2018

Encyclopedia of Life Sciences

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Climate disruption is an increasing pressure on food supply worldwide. Consequently, it is required to develop strategies to improve the yield of crops under abiotic stress as plants have to endure novel adverse environmental conditions. Among them, drought and salinity constrain agricultural productivity most dramatically. Many of the plant adaptive responses occur at the cell membrane. There, the communication between those processes that are disrupted as a consequence of the adverse environmental stimuli and those involved in the plant adaptive response is established. The available data show that this communication is achieved by a regulated localisation of different signalling molecules to the vicinity of ion channels and transporters. The structural characterisation of those complexes constitutes a major challenge to understand the mechanism to confer plant resistance to stress and to implement novel biotechnological approaches to ensure food security. Key Concepts The understanding at the molecular level of the mechanisms for plant adaptation to drought and salinity helps to implement novel biotechnological approaches to ensure food security. The cytosolic levels of the phytohormone abscisic acid (ABA) and the Ca 2+ ion (Ca 2+ ) act as a molecular switch to plant adaptive response to stress. Plant cell response to abiotic stress is mediated by supramolecular complexes that are formed in the vicinity or at the cell membrane. Structural biology has provided the bases for ABA and Ca 2+ roles as they affect the molecular architecture of the signalling complexes regulating plant response. The structural information can be used to drive a genetic approach and for the identification of small molecules that can be used as new agrochemicals for plant improvement.

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Identification and mechanism of ABA receptor antagonism

Cited by 150 publications

References 35 publications

The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs

Structural Biology of Salt and Drought Tolerance in Plants

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