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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
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    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.

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