Moss PIEZO homologs have a conserved structure, are ubiquitously expressed, and do not affect general vacuole function

Plant Signal Behav. 2022 Dec 31;17(1):2015893. doi: 10.1080/15592324.2021.2015893. Epub 2021 Dec 24.

Abstract

The PIEZO protein family was first described in animals where these mechanosensitive calcium channels perform numerous essential functions, including the perception of light touch, shear, and compressive forces. PIEZO homologs are present in most eukaryotic lineages and recently we reported that two PIEZO homologs from moss Physcomitrium patens localize to the vacuolar membrane and modulate its morphology in tip-growing caulonemal cells. Here we show that predicted structures of both PpPIEZO1 and PpPIEZO2 are very similar to that of mouse Piezo2. Furthermore, we show that both moss PIEZO genes are ubiquitously expressed in moss vegetative tissues and that they are not required for normal vacuolar pH or intracellular osmotic potential. These results suggest that moss PIEZO proteins are widely expressed mechanosensory calcium channels that serve a signaling rather than maintenance role in vacuoles.

Keywords: PIEZO; Physcomitrium; mechanosensitive ion channel; moss; vacuole.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Bryopsida* / genetics
  • Bryopsida* / metabolism
  • Ion Channels / genetics
  • Ion Channels / metabolism
  • Mechanotransduction, Cellular
  • Mice
  • Signal Transduction
  • Vacuoles* / metabolism

Substances

  • Ion Channels