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      Mechanosensitive Ion Channels: Structural Features Relevant to Mechanotransduction Mechanisms

      Author(s): 1 , 1 , 2 , 1 , 2
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      Journal: Annual Review of Neuroscience
      Publisher: Annual Reviews

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          Abstract

          Activation of mechanosensitive ion channels underlies a variety of fundamental physiological processes that require sensation of mechanical force. Different mechanosensitive channels adapt distinctive structures and mechanotransduction mechanisms to fit their biological roles. How mechanosensitive channels work, especially in animals, has been extensively studied in the past decade. Here we review key findings in the functional and structural characterizations of these channels and highlight the structural features relevant to the mechanotransduction mechanism of each specific channel.

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          Structure of the TRPV1 ion channel determined by electron cryo-microscopy

          Maofu Liao, Erhu Cao, David Julius … (2013)
          Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been hampered by a lack of detailed structural information. Here, we exploit advances in electron cryo-microscopy to determine the structure of a mammalian TRP channel, TRPV1, at 3.4Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Like voltage-gated channels, TRPV1 exhibits four-fold symmetry around a central ion pathway formed by transmembrane helices S5–S6 and the intervening pore loop, which is flanked by S1–S4 voltage sensor-like domains. TRPV1 has a wide extracellular ‘mouth’ with short selectivity filter. The conserved ‘TRP domain’ interacts with the S4–S5 linker, consistent with its contribution to allosteric modulation. Subunit organization is facilitated by interactions among cytoplasmic domains, including N-terminal ankyrin repeats. These observations provide a structural blueprint for understanding unique aspects of TRP channel function.
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            TRP channels as cellular sensors.

            David Clapham (2003)
            TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.
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              TMEM16A confers receptor-activated calcium-dependent chloride conductance.

              Young Duk Yang, Hawon Cho, Jae Koo … (2008)
              Calcium (Ca(2+))-activated chloride channels are fundamental mediators in numerous physiological processes including transepithelial secretion, cardiac and neuronal excitation, sensory transduction, smooth muscle contraction and fertilization. Despite their physiological importance, their molecular identity has remained largely unknown. Here we show that transmembrane protein 16A (TMEM16A, which we also call anoctamin 1 (ANO1)) is a bona fide Ca(2+)-activated chloride channel that is activated by intracellular Ca(2+) and Ca(2+)-mobilizing stimuli. With eight putative transmembrane domains and no apparent similarity to previously characterized channels, ANO1 defines a new family of ionic channels. The biophysical properties as well as the pharmacological profile of ANO1 are in full agreement with native Ca(2+)-activated chloride currents. ANO1 is expressed in various secretory epithelia, the retina and sensory neurons. Furthermore, knockdown of mouse Ano1 markedly reduced native Ca(2+)-activated chloride currents as well as saliva production in mice. We conclude that ANO1 is a candidate Ca(2+)-activated chloride channel that mediates receptor-activated chloride currents in diverse physiological processes.
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                Author and article information

                Journal
                Title: Annual Review of Neuroscience
                Abbreviated Title: Annu. Rev. Neurosci.
                Publisher: Annual Reviews
                ISSN (Print): 0147-006X
                ISSN (Electronic): 1545-4126
                Publication date Created: July 08 2020
                Publication date (Print): July 08 2020
                Volume: 43
                Issue: 1
                Pages: 207-229
                Affiliations
                [1 ]Department of Physiology, University of California, San Francisco, California 94158, USA;
                [2 ]Department of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, California 94158, USA
                Article
                DOI: 10.1146/annurev-neuro-070918-050509
                PubMed ID: 32084327
                SO-VID: 2eeb6bfd-d7ec-4767-84cb-17df8c7fedd9
                Copyright © © 2020
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