A G Protein-Coupled Receptor Is a Plasma Membrane Receptor for the Plant Hormone Abscisic Acid

Liu, Xigang; Yue, Yanling; Li, Bin; Nie, Yanli; Li, Wei; Wu, Weihua; Ma, Ligeng

doi:10.1126/science.1135882

Cited by 319 publications

(337 citation statements)

References 25 publications

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“…Recently, two putative ABA receptors have been identified on the basis of biochemical binding assays. One of these, a G-protein-coupled receptor, is located in the plasma membrane [61], although subsequent genetic characterization failed to confirm its role in the ABA response [62]. Another putative ABA receptor was identified as a chloroplast-located magnesium-chelatase that is involved in chlorophyll synthesis [63].…”

Section: How Do Plants Resist Pathogens?mentioning

confidence: 99%

The multifaceted role of ABA in disease resistance

Ton

Flors

Mauch‐Mani

2009

Trends in Plant Science

738

583

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Section: How Do Plants Resist Pathogens?mentioning

confidence: 99%

The multifaceted role of ABA in disease resistance

Ton

Flors

Mauch‐Mani

2009

Trends in Plant Science

738

583

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“…A plasma membranelocalized, putative G protein-coupled receptor has also been proposed to be an ABA receptor (X. Liu et al, 2007aLiu et al, , 2007b, in addition to the two soluble ABAbinding proteins, the Mg-chelatase and the FCA RNAbinding protein (Razem et al, 2006;Shen et al, 2006).…”

Section: Atpub Proteins and S-domainmentioning

confidence: 99%

Interactions between theS-Domain Receptor Kinases and AtPUB-ARM E3 Ubiquitin Ligases Suggest a Conserved Signaling Pathway in Arabidopsis

et al. 2008

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The Arabidopsis (Arabidopsis thaliana) genome encompasses multiple receptor kinase families with highly variable extracellular domains. Despite their large numbers, the various ligands and the downstream interacting partners for these kinases have been deciphered only for a few members. One such member, the S-receptor kinase, is known to mediate the self-incompatibility (SI) response in Brassica. S-receptor kinase has been shown to interact and phosphorylate a U-box/ARM-repeat-containing E3 ligase, ARC1, which, in turn, acts as a positive regulator of the SI response. In an effort to identify conserved signaling pathways in Arabidopsis, we performed yeast two-hybrid analyses of various S-domain receptor kinase family members with representative Arabidopsis plant U-box/ARM-repeat (AtPUB-ARM) E3 ligases. The kinase domains from S-domain receptor kinases were found to interact with ARM-repeat domains from AtPUB-ARM proteins. These kinase domains, along with M-locus protein kinase, a positive regulator of SI response, were also able to phosphorylate the ARM-repeat domains in in vitro phosphorylation assays. Subcellular localization patterns were investigated using transient expression assays in tobacco (Nicotiana tabacum) BY-2 cells and changes were detected in the presence of interacting kinases. Finally, potential links to the involvement of these interacting modules to the hormone abscisic acid (ABA) were investigated. Interestingly, AtPUB9 displayed redistribution to the plasma membrane of BY-2 cells when either treated with ABA or coexpressed with the active kinase domain of ARK1. As well, T-DNA insertion mutants for ARK1 and AtPUB9 lines were altered in their ABA sensitivity during germination and acted at or upstream of ABI3, indicating potential involvement of these proteins in ABA responses.

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“…The GPA1 G protein a subunit (Ga) has been shown to modulate ABA regulation of stomatal opening (Wang et al, 2001) and closure (Liu et al, 2007) and ExtCaM induction of stomatal closure . To investigate whether Ga also regulates ExtCaM induction of NO generation, we examined NO levels in guard cells of the gpa1 null mutants and of transgenic lines expressing a constitutively active form of GPA1 (cGa; Okamoto et al, 2001;Wang et al, 2001).…”

Section: G Protein a Subunit Modulates Atnoa1-dependent No Productionmentioning

confidence: 99%

“…Furthermore, ExtCaM triggers [Ca 2+ ] i elevation in guard cells of V. faba and Arabidopsis and in lily (Lilium daviddi) pollen Xiao et al, 2004;Shang et al, 2005 . G protein, Ca 2+ , and H 2 O 2 are well-known second messengers in ABA-induced guard cell signaling (McAinsh et al, 1995;Grabov and Blatt, 1998;Pei et al, 2000;Wang et al, 2001;Zhang et al, 2001;Liu et al, 2007). However, the signaling cascade triggered by ExtCaM in guard cells is poorly understood.…”

mentioning

confidence: 99%

A Signaling Pathway Linking Nitric Oxide Production to Heterotrimeric G Protein and Hydrogen Peroxide Regulates Extracellular Calmodulin Induction of Stomatal Closure in Arabidopsis

Liu

et al. 2009

Plant Physiology

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Extracellular calmodulin (ExtCaM) regulates stomatal movement by eliciting a cascade of intracellular signaling events including heterotrimeric G protein, hydrogen peroxide (H 2 O 2 ), and Ca 2+ . However, the ExtCaM-mediated guard cell signaling pathway remains poorly understood. In this report, we show that Arabidopsis (Arabidopsis thaliana) NITRIC OXIDE ASSOCIATED1 (AtNOA1)-dependent nitric oxide (NO) accumulation plays a crucial role in ExtCaM-induced stomatal closure. ExtCaM triggered a significant increase in NO levels associated with stomatal closure in the wild type, but both effects were abolished in the Atnoa1 mutant. Furthermore, we found that ExtCaM-mediated NO generation is regulated by GPA1, the Ga-subunit of heterotrimeric G protein. The ExtCaM-dependent NO accumulation was nullified in gpa1 knockout mutants but enhanced by overexpression of a constitutively active form of GPA1 (cGa). In addition, cGa Atnoa1 and gpa1-2 Atnoa1 double mutants exhibited a similar response as did Atnoa1. The defect in gpa1 was rescued by overexpression of AtNOA1. Finally, we demonstrated that G protein activation of NO production depends on H 2 O 2 . Reduced H 2 O 2 levels in guard cells blocked the stomatal response of cGa lines, whereas exogenously applied H 2 O 2 rescued the defect in ExtCaM-mediated stomatal closure in gpa1 mutants. Moreover, the atrbohD/F mutant, which lacks the NADPH oxidase activity in guard cells, had impaired NO generation in response to ExtCaM, and H 2 O 2 -induced stomatal closure and NO accumulation were greatly impaired in Atnoa1. These findings have established a signaling pathway leading to ExtCaM-induced stomatal closure, which involves GPA1-dependent activation of H 2 O 2 production and subsequent AtNOA1-dependent NO accumulation.Plant guard cells control opening and closure of the stomata in response to phytohormones (e.g. abscisic acid [ABA]) and various environmental signals such as light and temperature, thereby regulating gas exchange for photosynthesis and water status via transpiration . Cytosolic calcium ([Ca 2+ ] i ) has been shown to be a key second messenger that changes in response to multiple stimuli in guard cells (McAinsh et al., 1995;Grabov and Blatt, 1998;Wood et al., 2000). A large proportion of Ca 2+ is localized in extracellular space. It has been shown that external Ca 2+ concentration ([Ca 2+ ] o ) promotes stomatal closure and induces oscillation in [Ca 2+ ] i in guard cells (MacRobbie, 1992;McAinsh et al., 1995;Allen et al., 2001 Calmodulin is a well-known Ca 2+ sensor that is activated upon binding of Ca 2+ . It has been shown that calmodulin exists not only intracellularly but also extracellularly in many plant species

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A G Protein-Coupled Receptor Is a Plasma Membrane Receptor for the Plant Hormone Abscisic Acid

Cited by 319 publications

References 25 publications

The multifaceted role of ABA in disease resistance

The multifaceted role of ABA in disease resistance

Interactions between theS-Domain Receptor Kinases and AtPUB-ARM E3 Ubiquitin Ligases Suggest a Conserved Signaling Pathway in Arabidopsis

A Signaling Pathway Linking Nitric Oxide Production to Heterotrimeric G Protein and Hydrogen Peroxide Regulates Extracellular Calmodulin Induction of Stomatal Closure in Arabidopsis

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