Piezo channel mechanisms in health and disease

Piezo channel mechanisms in health and disease IntroductionPiezo proteins are large membrane proteins which assemble to form mechanically activated Ca2+‐permeable non‐selective cationic channels (Coste et al. , ; Murthy et al. ; Wu et al. ). They serve to regulate membrane potential and Ca2+ signalling coupled to downstream effectors such as calpain in cells of mammals and other classes (Coste et al. , ; Li et al. ; Murthy et al. ; Rode et al. ; Wu et al. ). They are a distinct type of ion channel subunit which assembles as trimers with a central ion‐conducting pore covered by a single cap and three complex arms reaching out into and curving the membrane (Ge et al. ; Guo & MacKinnon, ; Saotome et al. ; Zhao et al. ) (Fig. ). The last two C‐terminal transmembrane segments (TMs) form the functional pore module (Zhao et al. ) while the rest of the protein comprises nine repetitive units of four TMs assembled into a highly curved peripheral blade‐like structure which is critical for mechano‐sensing and transduction (Zhao et al. ; Fig. 1). The channels are inherent sensors of membrane tension and increases in this tension seem to be the primary physiological activator (Lewis & Grandl, ; Cox et al. ; Syeda et al. ). Activation or sensitisation to membrane tension occurs in response http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Physiology Wiley

Piezo channel mechanisms in health and disease

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Journal compilation © 2018 The Physiological Society
ISSN
0022-3751
eISSN
1469-7793
D.O.I.
10.1113/JP274395
Publisher site
See Article on Publisher Site

Abstract

IntroductionPiezo proteins are large membrane proteins which assemble to form mechanically activated Ca2+‐permeable non‐selective cationic channels (Coste et al. , ; Murthy et al. ; Wu et al. ). They serve to regulate membrane potential and Ca2+ signalling coupled to downstream effectors such as calpain in cells of mammals and other classes (Coste et al. , ; Li et al. ; Murthy et al. ; Rode et al. ; Wu et al. ). They are a distinct type of ion channel subunit which assembles as trimers with a central ion‐conducting pore covered by a single cap and three complex arms reaching out into and curving the membrane (Ge et al. ; Guo & MacKinnon, ; Saotome et al. ; Zhao et al. ) (Fig. ). The last two C‐terminal transmembrane segments (TMs) form the functional pore module (Zhao et al. ) while the rest of the protein comprises nine repetitive units of four TMs assembled into a highly curved peripheral blade‐like structure which is critical for mechano‐sensing and transduction (Zhao et al. ; Fig. 1). The channels are inherent sensors of membrane tension and increases in this tension seem to be the primary physiological activator (Lewis & Grandl, ; Cox et al. ; Syeda et al. ). Activation or sensitisation to membrane tension occurs in response

Journal

The Journal of PhysiologyWiley

Published: Jan 15, 2018

Keywords: ; ;

References

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