Piezo1 ion channel pore properties are dictated by C-terminal region - Archive ouverte HAL Access content directly
Journal Articles Nature Communications Year : 2015

Piezo1 ion channel pore properties are dictated by C-terminal region

(1, 2) , (2) , (3) , (2) , (1) , (1) , (3, 2)
1
2
3

Abstract

Piezo1 and Piezo2 encode mechanically activated cation channels that function as mechano-transducers involved in vascular system development and touch sensing, respectively. Structural features of Piezos remain unknown. Mouse Piezo1 is bioinformatically predicted to have 30–40 transmembrane (TM) domains. Here, we find that nine of the putative inter-transmembrane regions are accessible from the extracellular side. We use chimeras between mPiezo1 and dPiezo to show that ion-permeation properties are conferred by C-terminal region. We further identify a glutamate residue within a conserved region adjacent to the last two putative TM domains of the protein, that when mutated, affects unitary conductance and ion selectivity, and modulates pore block. We propose that this amino acid is either in the pore or closely associates with the pore. Our results describe important structural motifs of this channel family and lay the groundwork for a mechanistic understanding of how Piezos are mechanically gated and conduct ions.
Fichier principal
Vignette du fichier
ncomms8223.pdf (1.86 Mo) Télécharger le fichier
Origin : Explicit agreement for this submission
Loading...

Dates and versions

hal-01787362 , version 1 (07-05-2018)

Licence

Attribution - CC BY 4.0

Identifiers

Cite

Bertrand Coste, Swetha Murthy, Jayanti Mathur, Manuela Schmidt, Yasmine Mechioukhi, et al.. Piezo1 ion channel pore properties are dictated by C-terminal region. Nature Communications, 2015, 6 (1), ⟨10.1038/ncomms8223⟩. ⟨hal-01787362⟩
128 View
85 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More