IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v452y2008i7186d10.1038_nature06720.html
   My bibliography  Save this article

CO2 regulator SLAC1 and its homologues are essential for anion homeostasis in plant cells

Author

Listed:
  • Juntaro Negi

    (Faculty of Sciences, Kyushu University)

  • Osamu Matsuda

    (Faculty of Sciences, Kyushu University)

  • Takashi Nagasawa

    (Faculty of Sciences, Kyushu University)

  • Yasuhiro Oba

    (Faculty of Sciences, Kyushu University)

  • Hideyuki Takahashi

    (Iwate Biotechnology Center, Kitakami, Iwate 024-0003, Japan)

  • Maki Kawai-Yamada

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Hirofumi Uchimiya

    (Iwate Biotechnology Center, Kitakami, Iwate 024-0003, Japan
    Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Mimi Hashimoto

    (Faculty of Sciences, Kyushu University)

  • Koh Iba

    (Faculty of Sciences, Kyushu University)

Abstract

A stomatal ion channel The stomata on the undersides of leaves control the exchange of carbon dioxide and water between plants and the atmosphere. Stomatal pore aperture is regulated by transport of ions and metabolites across guard-cell membranes. Perhaps surprisingly, until now no plant plasma membrane anion channel subunits have been cloned — and the homologues of animal anion channels have been shown not to encode functional ion channels in plants. Now two groups working independently have identified a protein that is an essential component for S-type anion channel function and is required for stomatal closure in response to a variety of physiological and stress stimuli. Termed SLAC1, it is a distant homologue of fungal and bacterial dicarboxylate/malic acid transport proteins.

Suggested Citation

  • Juntaro Negi & Osamu Matsuda & Takashi Nagasawa & Yasuhiro Oba & Hideyuki Takahashi & Maki Kawai-Yamada & Hirofumi Uchimiya & Mimi Hashimoto & Koh Iba, 2008. "CO2 regulator SLAC1 and its homologues are essential for anion homeostasis in plant cells," Nature, Nature, vol. 452(7186), pages 483-486, March.
    • Handle: RePEc:nat:nature:v:452:y:2008:i:7186:d:10.1038_nature06720
    DOI: 10.1038/nature06720
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature06720
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature06720?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yawen Li & Yinan Ding & Lili Qu & Xinru Li & Qinxuan Lai & Pingxia Zhao & Yongxiang Gao & Chengbin Xiang & Chunlei Cang & Xin Liu & Linfeng Sun, 2022. "Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Yeongmok Lee & Hyeon Seong Jeong & Seoyeon Jung & Junmo Hwang & Chi Truc Han Le & Sung-Hoon Jun & Eun Jo Du & KyeongJin Kang & Beom-Gi Kim & Hyun-Ho Lim & Sangho Lee, 2023. "Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:452:y:2008:i:7186:d:10.1038_nature06720. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.