Response to Comment on "A G Protein–Coupled Receptor Is a Plasma Membrane Receptor for the Plant Hormone Abscisic Acid"

Liu, Xigang; Yue, Yanling; Li, Wei; Ma, Ligeng

doi:10.1126/science.1143320

Cited by 32 publications

(20 citation statements)

References 13 publications

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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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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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“…ABA signal transduction has been extensively studied, and numerous signaling components, including ABA receptors, have been identified (reviewed in Finkelstein and Rock 2002; Cutler et al 2010). A putative G-protein-coupled receptor GCR2 and GPCR-type G proteins GTG1 and GTG2 have been reported as candidate plasma membrane-type ABA receptors (Liu et al 2007a, b; Johnston et al 2007; Pandey et al 2009), though it is controversial whether GCR2 regulates ABA-mediated inhibition of seed germination and post-germination growth (Gao et al 2007; Guo et al 2008). GTGs are positively involved in ABA signaling and interacts with the sole Arabidopsis G protein α subunit GPA1 (Pandey and Assmann 2004), which inhibits the activity of GTG-ABA binding to negatively regulate ABA signaling (Pandey et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis

Zhang

Jiang

et al. 2013

Plant Mol Biol

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Previous study showed that the magnesium-protoporphyrin IX chelatase H subunit (CHLH/ABAR) positively regulates abscisic acid (ABA) signaling. Here, we investigated the functions of a CHLH/ABAR interaction protein, the chloroplast co-chaperonin 20 (CPN20) in ABA signaling in Arabidopsis thaliana. We showed that down-expression of the CPN20 gene increases, but overexpression of the CPN20 gene reduces, ABA sensitivity in the major ABA responses including ABA-induced seed germination inhibition, postgermination growth arrest, promotion of stomatal closure and inhibition of stomatal opening. Genetic evidence supports that CPN20 functions downstream or at the same node of CHLH/ABAR, but upstream of the WRKY40 transcription factor. The other CPN20 interaction partners CPN10 and CPN60 are not involved in ABA signaling. Our findings show that CPN20 functions negatively in the ABAR-WRKY40 coupled ABA signaling independently of its co-chaperonin role, and provide a new insight into the role of co-chaperones in the regulation of plant responses to environmental cues.Electronic supplementary materialThe online version of this article (doi:10.1007/s11103-013-0082-8) contains supplementary material, which is available to authorized users.

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“…ABA signal perception, which has been considered to be mediated by multiple receptors, including plasma membrane and intracellular receptors (for review, see Assmann, 1994;, has attracted much attention. In recent years, two classes of plasma membrane ABA receptors, an unconventional G-protein-coupled receptor (GPCR), GCR2, and a novel class of GPCR, GTG1 and GTG2, that regulate the major ABA responses in seed germination, seedling growth, and stomatal movement (Johnston et al, 2007;Liu et al, 2007aLiu et al, , 2007bPandey et al, 2009), have been reported. However, whether GCR2 regulates ABA-mediated seed germination and postgermination growth is controversial, because the ABA-related phenotypes are weak to absent in gcr2 mutants Guo et al, 2008).…”

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confidence: 99%

The Magnesium-Chelatase H Subunit Binds Abscisic Acid and Functions in Abscisic Acid Signaling: New Evidence in Arabidopsis

et al. 2009

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Using a newly developed abscisic acid (ABA)-affinity chromatography technique, we showed that the magnesium-chelatase H subunit ABAR/CHLH (for putative abscisic acid receptor/chelatase H subunit) specifically binds ABA through the C-terminal half but not the N-terminal half. A set of potential agonists/antagonists to ABA, including 2-trans,4-trans-ABA, gibberellin, cytokinin-like regulator 6-benzylaminopurine, auxin indole-3-acetic acid, auxin-like substance naphthalene acetic acid, and jasmonic acid methyl ester, did not bind ABAR/CHLH. A C-terminal C370 truncated ABAR with 369 amino acid residues (631-999) was shown to bind ABA, which may be a core of the ABA-binding domain in the C-terminal half. Consistently, expression of the ABAR/CHLH C-terminal half truncated proteins fused with green fluorescent protein (GFP) in wild-type plants conferred ABA hypersensitivity in all major ABA responses, including seed germination, postgermination growth, and stomatal movement, and the expression of the same truncated proteins fused with GFP in an ABA-insensitive cch mutant of the ABAR/CHLH gene restored the ABA sensitivity of the mutant in all of the ABA responses. However, the effect of expression of the ABAR N-terminal half fused with GFP in the wild-type plants was limited to seedling growth, and the restoring effect of the ABA sensitivity of the cch mutant was limited to seed germination. In addition, we identified two new mutant alleles of ABAR/CHLH from the mutant pool in the Arabidopsis Biological Resource Center via Arabidopsis (Arabidopsis thaliana) Targeting-Induced Local Lesions in Genomes. The abar-2 mutant has a point mutation resulting in the N-terminal Leu-348/ Phe, and the abar-3 mutant has a point mutation resulting in the N-terminal Ser-183/Phe. The two mutants show altered ABA-related phenotypes in seed germination and postgermination growth but not in stomatal movement. These findings support the idea that ABAR/CHLH is an ABA receptor and reveal that the C-terminal half of ABAR/CHLH plays a central role in ABA signaling, which is consistent with its ABA-binding ability, but the N-terminal half is also functionally required, likely through a regulatory action on the C-terminal half.

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Response to Comment on "A G Protein–Coupled Receptor Is a Plasma Membrane Receptor for the Plant Hormone Abscisic Acid"

Cited by 32 publications

References 13 publications

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

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

Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis

The Magnesium-Chelatase H Subunit Binds Abscisic Acid and Functions in Abscisic Acid Signaling: New Evidence in Arabidopsis

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