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      Closing Plant Stomata Requires a Homolog of an Aluminum-Activated Malate Transporter

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          Abstract

          Plant stomata limit both carbon dioxide uptake and water loss; hence, stomatal aperture is carefully set as the environment fluctuates. Aperture area is known to be regulated in part by ion transport, but few of the transporters have been characterized. Here we report that AtALMT12 (At4g17970), a homolog of the aluminum-activated malate transporter (ALMT) of wheat, is expressed in guard cells of Arabidopsis thaliana. Loss-of-function mutations in AtALMT12 impair stomatal closure induced by ABA, calcium and darkness, but do not abolish either the rapidly activated or the slowly activated anion currents previously identified as being important for stomatal closure. Expressed in Xenopus oocytes, AtALMT12 facilitates chloride and nitrate currents, but not those of organic solutes. Therefore, we conclude that AtALMT12 is a novel class of anion transporter involved in stomatal closure.

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          NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signaling in Arabidopsis.

          June M. Kwak, Izumi C. Mori, Zhen-Ming Pei … (2003)
          Reactive oxygen species (ROS) have been proposed to function as second messengers in abscisic acid (ABA) signaling in guard cells. However, the question whether ROS production is indeed required for ABA signal transduction in vivo has not yet been addressed, and the molecular mechanisms mediating ROS production during ABA signaling remain unknown. Here, we report identification of two partially redundant Arabidopsis guard cell-expressed NADPH oxidase catalytic subunit genes, AtrbohD and AtrbohF, in which gene disruption impairs ABA signaling. atrbohD/F double mutations impair ABA-induced stomatal closing, ABA promotion of ROS production, ABA-induced cytosolic Ca(2+) increases and ABA- activation of plasma membrane Ca(2+)-permeable channels in guard cells. Exogenous H(2)O(2) rescues both Ca(2+) channel activation and stomatal closing in atrbohD/F. ABA inhibition of seed germination and root elongation are impaired in atrbohD/F, suggesting more general roles for ROS and NADPH oxidases in ABA signaling. These data provide direct molecular genetic and cell biological evidence that ROS are rate-limiting second messengers in ABA signaling, and that the AtrbohD and AtrbohF NADPH oxidases function in guard cell ABA signal transduction.
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            Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair.

            Dietmar Geiger, Sönke Scherzer, Patrick Mumm … (2009)
            In response to drought stress the phytohormone ABA (abscisic acid) induces stomatal closure and, therein, activates guard cell anion channels in a calcium-dependent as well as-independent manner. Two key components of the ABA signaling pathway are the protein kinase OST1 (open stomata 1) and the protein phosphatase ABI1 (ABA insensitive 1). The recently identified guard cell anion channel SLAC1 appeared to be the key ion channel in this signaling pathway but remained electrically silent when expressed heterologously. Using split YFP assays, we identified OST1 as an interaction partner of SLAC1 and ABI1. Upon coexpression of SLAC1 with OST1 in Xenopus oocytes, SLAC1-related anion currents appeared similar to those observed in guard cells. Integration of ABI1 into the SLAC1/OST1 complex, however, prevented SLAC1 activation. Our studies demonstrate that SLAC1 represents the slow, deactivating, weak voltage-dependent anion channel of guard cells controlled by phosphorylation/dephosphorylation.
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              SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling.

              Triin Vahisalu, Hannes Kollist, Yong-Fei Wang … (2008)
              Stomatal pores, formed by two surrounding guard cells in the epidermis of plant leaves, allow influx of atmospheric carbon dioxide in exchange for transpirational water loss. Stomata also restrict the entry of ozone--an important air pollutant that has an increasingly negative impact on crop yields, and thus global carbon fixation and climate change. The aperture of stomatal pores is regulated by the transport of osmotically active ions and metabolites across guard cell membranes. Despite the vital role of guard cells in controlling plant water loss, ozone sensitivity and CO2 supply, the genes encoding some of the main regulators of stomatal movements remain unknown. It has been proposed that guard cell anion channels function as important regulators of stomatal closure and are essential in mediating stomatal responses to physiological and stress stimuli. However, the genes encoding membrane proteins that mediate guard cell anion efflux have not yet been identified. Here we report the mapping and characterization of an ozone-sensitive Arabidopsis thaliana mutant, slac1. We show that SLAC1 (SLOW ANION CHANNEL-ASSOCIATED 1) is preferentially expressed in guard cells and encodes a distant homologue of fungal and bacterial dicarboxylate/malic acid transport proteins. The plasma membrane protein SLAC1 is essential for stomatal closure in response to CO2, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic Ca2+ and abscisic acid, but do not affect rapid (R-type) anion channel currents or Ca2+ channel function. A low homology of SLAC1 to bacterial and fungal organic acid transport proteins, and the permeability of S-type anion channels to malate suggest a vital role for SLAC1 in the function of S-type anion channels.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Plant Cell Physiol
                Journal ID (publisher-id): pcp
                Journal ID (hwp): pcellphys
                Title: Plant and Cell Physiology
                Publisher: Oxford University Press
                ISSN (Print): 0032-0781
                ISSN (Electronic): 1471-9053
                Publication date (Print): March 2010
                Publication date (Electronic): 11 February 2010
                Publication date PMC-release: 11 February 2010
                Volume: 51
                Issue: 3
                Pages: 354-365
                Affiliations
                1Research Institute for Bioresources, Okayama University, Chuo 2-20-1, Kurashiki, Okayama, 710-0046 Japan
                2Graduate School of Natural Science and Technology, Okayama University, Tsushima-Naka, Okayama, 700-8530 Japan
                3RIKEN Plant Science Center, Tsurumi-ku, Yokohama, 230-0045 Japan
                4Laboratory of Plant Nutrition, Faculty of Agriculture, Kyushu University, Higashi-ku, Fukuoka, 812-8581 Japan
                5These authors contributed equally to this work
                Author notes
                *Corresponding author: E-mail, tsasaki@ 123456rib.okayama-u.ac.jp ; Fax, +81-86-434-1236
                Article
                Publisher ID: pcq016
                DOI: 10.1093/pcp/pcq016
                PMC ID: 2835873
                PubMed ID: 20154005
                SO-VID: f019d211-dd6d-4cd1-926b-5bcf88e23e23
                Copyright © © The Author 2010. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 18 January 2010
                Date accepted : 9 February 2010
                Categories
                Subject: Rapid Papers

                ScienceOpen disciplines: Plant science & Botany
                Keywords: atalmt12,almt family protein,anion transporter,stomatal closure
                Data availability:
                ScienceOpen disciplines: Plant science & Botany
                Keywords: atalmt12, almt family protein, anion transporter, stomatal closure

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