Piezo1-dependent stretch-activated channels are inhibited by Polycystin-2 in renal tubular epithelial cells

EMBO Rep. 2013 Dec;14(12):1143-8. doi: 10.1038/embor.2013.170. Epub 2013 Oct 25.

Abstract

Mechanical forces associated with fluid flow and/or circumferential stretch are sensed by renal epithelial cells and contribute to both adaptive or disease states. Non-selective stretch-activated ion channels (SACs), characterized by a lack of inactivation and a remarkably slow deactivation, are active at the basolateral side of renal proximal convoluted tubules. Knockdown of Piezo1 strongly reduces SAC activity in proximal convoluted tubule epithelial cells. Similarly, overexpression of Polycystin-2 (PC2) or, to a greater extent its pathogenic mutant PC2-740X, impairs native SACs. Moreover, PC2 inhibits exogenous Piezo1 SAC activity. PC2 coimmunoprecipitates with Piezo1 and deletion of its N-terminal domain prevents both this interaction and inhibition of SAC activity. These findings indicate that renal SACs depend on Piezo1, but are critically conditioned by PC2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Action Potentials
  • Animals
  • Binding Sites
  • COS Cells
  • Cells, Cultured
  • Chlorocebus aethiops
  • Epithelial Cells / metabolism*
  • Epithelial Cells / physiology
  • Ion Channels / metabolism*
  • Kidney Tubules / cytology
  • Mechanotransduction, Cellular*
  • Mutation
  • Protein Binding
  • TRPC Cation Channels / metabolism
  • TRPP Cation Channels / chemistry
  • TRPP Cation Channels / genetics
  • TRPP Cation Channels / metabolism*

Substances

  • Ion Channels
  • PIEZO1 protein, human
  • TRPC Cation Channels
  • TRPP Cation Channels
  • polycystic kidney disease 2 protein