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MCAs in Arabidopsis are Ca2+-permeable mechanosensitive channels inherently sensitive to membrane tension

Author

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  • Kenjiro Yoshimura

    (Shibaura Institute of Technology)

  • Kazuko Iida

    (Tokyo Gakugei University
    Tokyo Metropolitan Institute of Medical Science)

  • Hidetoshi Iida

    (Tokyo Gakugei University)

Abstract

Mechanosensitive (MS) ion channels respond to mechanical stress and convert it into intracellular electric and ionic signals. Five MS channel families have been identified in plants, including the Mid1-Complementing Activity (MCA) channel; however, its activation mechanisms have not been elucidated in detail. We herein demonstrate that the MCA2 channel is a Ca2+-permeable MS channel that is directly activated by membrane tension. The N-terminal 173 residues of MCA1 and MCA2 were synthesized in vitro, purified, and reconstituted into artificial liposomal membranes. Liposomes reconstituted with MCA1(1-173) or MCA2(1-173) mediate Ca2+ influx and the application of pressure to the membrane reconstituted with MCA2(1-173) elicits channel currents. This channel is also activated by voltage. Blockers for MS channels inhibit activation by stretch, but not by voltage. Since MCA proteins are found exclusively in plants, these results suggest that MCA represent plant-specific MS channels that open directly with membrane tension.

Suggested Citation

  • Kenjiro Yoshimura & Kazuko Iida & Hidetoshi Iida, 2021. "MCAs in Arabidopsis are Ca2+-permeable mechanosensitive channels inherently sensitive to membrane tension," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26363-z
    DOI: 10.1038/s41467-021-26363-z
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    References listed on IDEAS

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    1. Yoshitaka Nakayama & Kenjiro Yoshimura & Hidetoshi Iida, 2012. "Organellar mechanosensitive channels in fission yeast regulate the hypo-osmotic shock response," Nature Communications, Nature, vol. 3(1), pages 1-10, January.
    2. Eduardo Perozo & D. Marien Cortes & Pornthep Sompornpisut & Anna Kloda & Boris Martinac, 2002. "Open channel structure of MscL and the gating mechanism of mechanosensitive channels," Nature, Nature, vol. 418(6901), pages 942-948, August.
    3. Kei Saotome & Swetha E. Murthy & Jennifer M. Kefauver & Tess Whitwam & Ardem Patapoutian & Andrew B. Ward, 2018. "Structure of the mechanically activated ion channel Piezo1," Nature, Nature, vol. 554(7693), pages 481-486, February.
    4. Fang Yuan & Huimin Yang & Yan Xue & Dongdong Kong & Rui Ye & Chijun Li & Jingyuan Zhang & Lynn Theprungsirikul & Tayler Shrift & Bryan Krichilsky & Douglas M. Johnson & Gary B. Swift & Yikun He & Jame, 2014. "OSCA1 mediates osmotic-stress-evoked Ca2+ increases vital for osmosensing in Arabidopsis," Nature, Nature, vol. 514(7522), pages 367-371, October.
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    Cited by:

    1. Jingying Zhang & Grigory Maksaev & Peng Yuan, 2023. "Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    2. Chang Zhao & Parker D. Webster & Alexis Angeli & Francesco Tombola, 2023. "Mechanically-primed voltage-gated proton channels from angiosperm plants," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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