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Piezo proteins are pore-forming subunits of mechanically activated channels

Academic Article
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Overview

related to degree

  • Kim, Sung Eun, Ph.D. in Biology, Scripps Research 2008 - 2013

authors

  • Coste, B.
  • Xiao, B. L.
  • Santos, J. S.
  • Syeda, R.
  • Grandl, J.
  • Spencer, K. S.
  • Kim, Sung Eun
  • Schmidt, M.
  • Mathur, J.
  • Dubin, Adrienne
  • Montal, M.
  • Patapoutian, Ardem

publication date

  • March 2012

journal

  • Nature  Journal

abstract

  • Mechanotransduction has an important role in physiology. Biological processes including sensing touch and sound waves require as-yet-unidentified cation channels that detect pressure. Mouse Piezo1 (MmPiezo1) and MmPiezo2 (also called Fam38a and Fam38b, respectively) induce mechanically activated cationic currents in cells; however, it is unknown whether Piezo proteins are pore-forming ion channels or modulate ion channels. Here we show that Drosophila melanogaster Piezo (DmPiezo, also called CG8486) also induces mechanically activated currents in cells, but through channels with remarkably distinct pore properties including sensitivity to the pore blocker ruthenium red and single channel conductances. MmPiezo1 assembles as a ∼1.2-million-dalton homo-oligomer, with no evidence of other proteins in this complex. Purified MmPiezo1 reconstituted into asymmetric lipid bilayers and liposomes forms ruthenium-red-sensitive ion channels. These data demonstrate that Piezo proteins are an evolutionarily conserved ion channel family involved in mechanotransduction.

subject areas

  • Animals
  • Drosophila Proteins
  • Drosophila melanogaster
  • Electric Conductivity
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Ion Channel Gating
  • Ion Channels
  • Lipid Bilayers
  • Mechanotransduction, Cellular
  • Mice
  • Molecular Sequence Data
  • NIH 3T3 Cells
  • Porosity
  • Protein Multimerization
  • Protein Subunits
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Identity

PubMed Central ID

  • PMC3297710

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/nature10812

PubMed ID

  • 22343900
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Additional Document Info

start page

  • 176

end page

  • 181

volume

  • 483

issue

  • 7388

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