Structure of the mechanically activated ion channel Piezo1 View Full Text


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Article Info

DATE

2017-12-20

AUTHORS

Kei Saotome, Swetha E. Murthy, Jennifer M. Kefauver, Tess Whitwam, Ardem Patapoutian, Andrew B. Ward

ABSTRACT

Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezo proteins are distinct from other ion channels and their structure remains poorly defined, which impedes detailed study of their gating and ion permeation properties. Here we report a high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer. The detergent-solubilized complex adopts a three-bladed propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-transmembrane helical bundles that we term Piezo repeats. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically. The structure provides a foundation to dissect further how Piezo channels are regulated by mechanical force. More... »

PAGES

481-486

References to SciGraph publications

  • 2015-11-09. The role of lipids in mechanosensation in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2013-05-21. Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels in NATURE COMMUNICATIONS
  • 2009-07. Crystal structure of the ATP-gated P2X4 ion channel in the closed state in NATURE
  • 2015-09-21. Architecture of the mammalian mechanosensitive Piezo1 channel in NATURE
  • 2016-09-14. X-ray structures define human P2X3 receptor gating cycle and antagonist action in NATURE
  • 2016-10-03. Localized force application reveals mechanically sensitive domains of Piezo1 in NATURE COMMUNICATIONS
  • 2013-12-04. Structure of the TRPV1 ion channel determined by electron cryo-microscopy in NATURE
  • 2014-12-03. Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel in NATURE
  • 2017-02-27. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy in NATURE METHODS
  • 2016-12-21. Piezo2 senses airway stretch and mediates lung inflation-induced apnoea in NATURE
  • 2012-02-19. The role of Drosophila Piezo in mechanical nociception in NATURE
  • 2015-05-26. Piezo1 ion channel pore properties are dictated by C-terminal region in NATURE COMMUNICATIONS
  • 2016-12-15. Recessive PIEZO2 stop mutation causes distal arthrogryposis with distal muscle weakness, scoliosis and proprioception defects in JOURNAL OF HUMAN GENETICS
  • 2007-09. Structure of acid-sensing ion channel 1 at 1.9 Å resolution and low pH in NATURE
  • 2008. Role of Lipid Bilayer Mechanics in Mechanosensation in MECHANOSENSITIVE ION CHANNELS
  • 2014-08-10. Piezo1 integration of vascular architecture with physiological force in NATURE
  • 2015-09-21. Impaired PIEZO1 function in patients with a novel autosomal recessive congenital lymphatic dysplasia in NATURE COMMUNICATIONS
  • 2016-06-22. The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels in NATURE COMMUNICATIONS
  • 2015-11-09. Piezo2 is the principal mechanotransduction channel for proprioception in NATURE NEUROSCIENCE
  • 2016-01-20. Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension in NATURE COMMUNICATIONS
  • 2015-08-17. EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy in NATURE METHODS
  • 2014-12-03. Piezo2 is the major transducer of mechanical forces for touch sensation in mice in NATURE
  • 2012-02-19. Piezo proteins are pore-forming subunits of mechanically activated channels in NATURE
  • 2009-05-20. Emerging roles for lipids in shaping membrane-protein function in NATURE
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    44 schema:description Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezo proteins are distinct from other ion channels and their structure remains poorly defined, which impedes detailed study of their gating and ion permeation properties. Here we report a high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer. The detergent-solubilized complex adopts a three-bladed propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-transmembrane helical bundles that we term Piezo repeats. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically. The structure provides a foundation to dissect further how Piezo channels are regulated by mechanical force.
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