Piezo proteins are pore-forming subunits of mechanically activated channels

Bertrand Coste, Bailong Xiao, Jose S. Santos, Ruhma Syeda, Jörg Grandl, Kathryn S. Spencer, Sung Eun Kim, Manuela Schmidt, Jayanti Mathur, Adrienne E. Dubin, Mauricio Montal () and Ardem Patapoutian ()
Additional contact information
Bertrand Coste: Dorris Neuroscience Center, The Scripps Research Institute
Bailong Xiao: Dorris Neuroscience Center, The Scripps Research Institute
Jose S. Santos: Section of Neurobiology, University of California San Diego
Ruhma Syeda: Section of Neurobiology, University of California San Diego
Jörg Grandl: Dorris Neuroscience Center, The Scripps Research Institute
Kathryn S. Spencer: Dorris Neuroscience Center, The Scripps Research Institute
Sung Eun Kim: Dorris Neuroscience Center, The Scripps Research Institute
Manuela Schmidt: Dorris Neuroscience Center, The Scripps Research Institute
Jayanti Mathur: Genomic Institute of the Novartis Research Foundation
Adrienne E. Dubin: Dorris Neuroscience Center, The Scripps Research Institute
Mauricio Montal: Section of Neurobiology, University of California San Diego
Ardem Patapoutian: Dorris Neuroscience Center, The Scripps Research Institute

Nature, 2012, vol. 483, issue 7388, 176-181

Abstract: 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.

Date: 2012
References: Add references at CitEc
Citations: View citations in EconPapers (13)

Downloads: (external link)
https://www.nature.com/articles/nature10812 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:483:y:2012:i:7388:d:10.1038_nature10812

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature10812

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().