Piezo proteins are pore-forming subunits of mechanically activated channels.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Coste, B; Xiao, B; Santos, JS; Syeda, R; Grandl, J; Spencer, KS; Kim, SE; Schmidt, M; Mathur, J; Dubin, AE; Montal, M; Patapoutian, A

Published Date

  • February 19, 2012

Published In

Volume / Issue

  • 483 / 7388

Start / End Page

  • 176 - 181

PubMed ID

  • 22343900

Pubmed Central ID

  • PMC3297710

Electronic International Standard Serial Number (EISSN)

  • 1476-4687

Digital Object Identifier (DOI)

  • 10.1038/nature10812


  • eng

Conference Location

  • England