A DTX/MATE-Type Transporter Facilitates Abscisic Acid Efflux and Modulates ABA Sensitivity and Drought Tolerance in Arabidopsis

Zhang, Haiwen; Zhu, Huifen; Pan, Ya‐Jun; Yu, Yuexuan; Luan, Sheng; Li, Legong

doi:10.1093/mp/ssu063

Cited by 239 publications

(220 citation statements)

References 35 publications

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“…3 D and E). The DTX33 and DTX35 transporters were not significantly permeable to organic acids, including citric acid and malate, in contrast to the MATE transporters described previously, including those mediating aluminum tolerance (18)(19)(20)(21)(22)29). It is noteworthy that both DTX members are slightly permeable to nitrate, which can be an abundant inorganic anion in plant cells under certain soil conditions.…”

Section: Resultsmentioning

confidence: 57%

“…We then measured the transport activity of isolated vacuoles from fluorescence-labeled cells by patch-clamp procedure (28). Several studies indicated that DTX/ MATE-type proteins transport organic acids, such as citric acid (18)(19)(20)(21)(22)29). We examined the possibility that DTX33 and DTX35 may function as anion transporters, like those reported earlier.…”

Section: Resultsmentioning

confidence: 94%

“…The EDS5 protein plays a role in the salicylic acid (SA)-dependent pathogen response pathway and possibly functions as an SA transporter responsible for SA release from chloroplasts (19,20). Our previous work indicates that AtDTX50 may serve as an abscisic acid (ABA) efflux transporter (21). A Significance Turgor pressure is the driving force for cell growth in plants, and the large central vacuole provides the major space for turgor regulation.…”

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confidence: 99%

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Two tonoplast MATE proteins function as turgor-regulating chloride channels in Arabidopsis

Zhang

Zhao

Tang

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The central vacuole in a plant cell occupies the majority of the cellular volume and plays a key role in turgor regulation. The vacuolar membrane (tonoplast) contains a large number of transporters that mediate fluxes of solutes and water, thereby adjusting cell turgor in response to developmental and environmental signals. We report that two tonoplast Detoxification efflux carrier (DTX)/Multidrug and Toxic Compound Extrusion (MATE) transporters, DTX33 and DTX35, function as chloride channels essential for turgor regulation in Arabidopsis. Ectopic expression of each transporter in Nicotiana benthamiana mesophyll cells elicited a large voltage-dependent inward chloride current across the tonoplast, showing that DTX33 and DTX35 each constitute a functional channel. Both channels are highly expressed in Arabidopsis tissues, including root hairs and guard cells that experience rapid turgor changes during root-hair elongation and stomatal movements. Disruption of these two genes, either in single or double mutants, resulted in shorter root hairs and smaller stomatal aperture, with double mutants showing more severe defects, suggesting that these two channels function additively to facilitate anion influx into the vacuole during cell expansion. In addition, dtx35 single mutant showed lower fertility as a result of a defect in pollen-tube growth. Indeed, patch-clamp recording of isolated vacuoles indicated that the inward chloride channel activity across the tonoplast was impaired in the double mutant. Because MATE proteins are widely known transporters of organic compounds, finding MATE members as chloride channels expands the functional definition of this large family of transporters.vacuole | root hair | stomata | drought

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Section: Resultsmentioning

confidence: 57%

Section: Resultsmentioning

confidence: 94%

mentioning

confidence: 99%

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Two tonoplast MATE proteins function as turgor-regulating chloride channels in Arabidopsis

Zhang

Zhao

Tang

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…However, recent studies have identified MATE transporters that are localized to plasma membrane, chloroplast, endomembrane systems (Li et al, 2002;Burko et al, 2011;Seo et al, 2012;Serrano et al, 2013;Li et al, 2014;Zhang et al, 2014). To determine to which membrane system the BIGE1 MATE transporter is localized, maize BIGE1 was fused with GFP at the C terminus and expressed under the control of the 35S promoter in stably transformed Arabidopsis.…”

Section: Subcellular Localization Of the Bige1 Mate Transportermentioning

confidence: 99%

Conserved Functions of the MATE Transporter BIG EMBRYO1 in Regulation of Lateral Organ Size and Initiation Rate

Suzuki

Satō

et al. 2015

The Plant Cell

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Genetic networks that determine rates of organ initiation and organ size are key regulators of plant architecture. Whereas several genes that influence the timing of lateral organ initiation have been identified, the regulatory pathways in which these genes operate are poorly understood. Here, we identify a class of genes implicated in regulation of the lateral organ initiation rate. Loss-of-function mutations in the MATE transporter encoded by maize (Zea mays) Big embryo 1 (Bige1) cause accelerated leaf and root initiation as well as enlargement of the embryo scutellum. BIGE1 is localized to trans-Golgi, indicating a possible role in secretion of a signaling molecule. Interestingly, phenotypes of bige1 bear striking similarity to cyp78a mutants identified in diverse plant species. We show that a CYP78A gene is upregulated in bige1 mutant embryos, suggesting a role for BIGE1 in feedback regulation of a CYP78A pathway. We demonstrate that accelerated leaf formation and early flowering phenotypes conditioned by mutants of Arabidopsis thaliana BIGE1 orthologs are complemented by maize Bige1, showing that the BIGE1 transporter has a conserved function in regulation of lateral organ initiation in plants. We propose that BIGE1 is required for transport of an intermediate or product associated with the CYP78A pathway.

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“…These transporters are involved in ABA efflux and influx with tissue-specific expression. Very recently, an Arabidopsis DTX/MATE family member, DTX50, has been shown to function as a mediator of ABA efflux (9).…”

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confidence: 99%

Abscisic Acid Transport in Human Erythrocytes

Vigliarolo¹,

Guida²,

Millo³

et al. 2015

Journal of Biological Chemistry

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Background:The plant stress hormone abscisic acid (ABA) is present and active in mammalian cells. Results: Band 3 protein is required for ABA influx into red blood cells (RBC); intracellular ABA activates adenylate cyclase resulting in [cAMP] i increase and subsequent ATP release. Conclusion: ABA influx through Band 3 activates ATP release from RBC. Significance: Paracrine ABA may regulate the ATP-mediated vasodilator response to inflammation.

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A DTX/MATE-Type Transporter Facilitates Abscisic Acid Efflux and Modulates ABA Sensitivity and Drought Tolerance in Arabidopsis

Cited by 239 publications

References 35 publications

Two tonoplast MATE proteins function as turgor-regulating chloride channels in Arabidopsis

Two tonoplast MATE proteins function as turgor-regulating chloride channels in Arabidopsis

Conserved Functions of the MATE Transporter BIG EMBRYO1 in Regulation of Lateral Organ Size and Initiation Rate

Abscisic Acid Transport in Human Erythrocytes

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