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

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.

journal_name

Nature

journal_title

Nature

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

doi

10.1038/nature10812

subject

Has Abstract

pub_date

2012-02-19 00:00:00

pages

176-81

issue

7388

eissn

0028-0836

issn

1476-4687

pii

nature10812

journal_volume

483

pub_type

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