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Selectivity mechanism of the mechanosensitive channel MscS revealed by probing channel subconducting states

Author

Listed:
  • C. D. Cox

    (School of Pharmacy and Pharmaceutical Sciences, Cardiff University)

  • T. Nomura

    (Victor Chang Cardiac Research Institute)

  • C. S. Ziegler

    (Centre for Drug Research, Ludwig-Maximilians-Universität München)

  • A. K. Campbell

    (School of Pharmacy and Pharmaceutical Sciences, Cardiff University)

  • K. T. Wann

    (School of Pharmacy and Pharmaceutical Sciences, Cardiff University)

  • B. Martinac

    (Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, University of New South Wales)

Abstract

The mechanosensitive channel of small conductance (MscS) has been characterized at both functional and structural levels and has an integral role in the protection of bacterial cells against hypoosmotic shock. Here we investigate the role that the cytoplasmic domain has in MscS channel function by recording wild-type and mutant MscS single-channel activity in liposome patches. We report that MscS preferentially resides in subconducting states at hyperpolarising potentials when Ca2+ and Ba2+ ions are the major permeant cations. In addition, our results indicate that charged residues proximal to the seven vestibular portals and their electrostatic interactions with permeating cations determine selectivity and regulate the conductance of MscS and potentially other channels belonging to the MscS subfamily. Furthermore, our findings suggest a role for mechanosensitive channels in bacterial calcium regulation, indicative of functions other than protection against osmolarity changes that these channels possibly fulfil in bacteria.

Suggested Citation

  • C. D. Cox & T. Nomura & C. S. Ziegler & A. K. Campbell & K. T. Wann & B. Martinac, 2013. "Selectivity mechanism of the mechanosensitive channel MscS revealed by probing channel subconducting states," Nature Communications, Nature, vol. 4(1), pages 1-11, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3137
    DOI: 10.1038/ncomms3137
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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. Jonathan Mount & Grigory Maksaev & Brock T. Summers & James A. J. Fitzpatrick & Peng Yuan, 2022. "Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Sebastian Jojoa-Cruz & Kei Saotome & Che Chun Alex Tsui & Wen-Hsin Lee & Mark S. P. Sansom & Swetha E. Murthy & Ardem Patapoutian & Andrew B. Ward, 2022. "Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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