Human aquaporin-11 guarantees efficient transport of H2O2 across the endoplasmic reticulum membrane
2019; Elsevier BV; Volume: 28; Linguagem: Inglês
10.1016/j.redox.2019.101326
ISSN2213-2317
AutoresStefano Bestetti, M Galli, Ilaria Sorrentino, Paolo Pinton, Alessandro Rimessi, Roberto Sitia, Iria Medraño-Fernández,
Tópico(s)ATP Synthase and ATPases Research
ResumoHydrogen 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.
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