Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane Articles uri icon

publication date

  • January 2020

start page

  • 1

end page

  • 7

issue

  • 101326

volume

  • 28

International Standard Serial Number (ISSN)

  • 2213-2317

abstract

  • Hydrogen peroxide (H2O2) is an essential second intracellular messenger. To reach its targets in the cytosol, H2O2 must cross a membrane, a feat that requires aquaporins (AQP) endowed with 'peroxiporin' activity (AQP3, AQP8, AQP9). Here, we exploit different organelle-targeted H2O2-sensitive probes to show that also AQP11 efficiently conduits H2O2. Unlike other peroxiporins, AQP11 is localized in the endoplasmic reticulum (ER), accumulating partly in mitochondrial-associated ER membranes (MAM). Its downregulation severely perturbs the flux of H2O2 through the ER, but not through the mitochondrial or plasma membranes. These properties make AQP11 a potential regulator of ER redox homeostasis and signaling.

subjects

  • Biology and Biomedicine
  • Materials science and engineering

keywords

  • aquaporins; peroxiporins; hydrogen peroxide; membrane permeability; endoplasmic reticulum; redox homeostasis