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
The Journal of Physiology – Wiley
Published: Jan 15, 2018
Keywords: ; ;
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