Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane

Hydrogen peroxide (H(2)O(2)) is an essential second intracellular messenger. To reach its targets in the cytosol, H(2)O(2) must cross a membrane, a feat that requires aquaporins (AQP) endowed with ‘peroxiporin’ activity (AQP3, AQP8, AQP9). Here, we exploit different organelle-targeted H(2)O(2)-sensi...

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Autores principales: Bestetti, Stefano, Galli, Mauro, Sorrentino, Ilaria, Pinton, Paolo, Rimessi, Alessandro, Sitia, Roberto, Medraño-Fernandez, Iria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6812059/
https://www.ncbi.nlm.nih.gov/pubmed/31546170
http://dx.doi.org/10.1016/j.redox.2019.101326
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author Bestetti, Stefano
Galli, Mauro
Sorrentino, Ilaria
Pinton, Paolo
Rimessi, Alessandro
Sitia, Roberto
Medraño-Fernandez, Iria
author_facet Bestetti, Stefano
Galli, Mauro
Sorrentino, Ilaria
Pinton, Paolo
Rimessi, Alessandro
Sitia, Roberto
Medraño-Fernandez, Iria
author_sort Bestetti, Stefano
collection PubMed
description Hydrogen peroxide (H(2)O(2)) is an essential second intracellular messenger. To reach its targets in the cytosol, H(2)O(2) must cross a membrane, a feat that requires aquaporins (AQP) endowed with ‘peroxiporin’ activity (AQP3, AQP8, AQP9). Here, we exploit different organelle-targeted H(2)O(2)-sensitive probes to show that also AQP11 efficiently conduits H(2)O(2). 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 H(2)O(2) 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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spelling pubmed-68120592019-10-30 Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane Bestetti, Stefano Galli, Mauro Sorrentino, Ilaria Pinton, Paolo Rimessi, Alessandro Sitia, Roberto Medraño-Fernandez, Iria Redox Biol Research Paper Hydrogen peroxide (H(2)O(2)) is an essential second intracellular messenger. To reach its targets in the cytosol, H(2)O(2) must cross a membrane, a feat that requires aquaporins (AQP) endowed with ‘peroxiporin’ activity (AQP3, AQP8, AQP9). Here, we exploit different organelle-targeted H(2)O(2)-sensitive probes to show that also AQP11 efficiently conduits H(2)O(2). 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 H(2)O(2) through the ER, but not through the mitochondrial or plasma membranes. These properties make AQP11 a potential regulator of ER redox homeostasis and signaling. Elsevier 2019-09-12 /pmc/articles/PMC6812059/ /pubmed/31546170 http://dx.doi.org/10.1016/j.redox.2019.101326 Text en © 2019 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Paper
Bestetti, Stefano
Galli, Mauro
Sorrentino, Ilaria
Pinton, Paolo
Rimessi, Alessandro
Sitia, Roberto
Medraño-Fernandez, Iria
Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title_full Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title_fullStr Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title_full_unstemmed Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title_short Human aquaporin-11 guarantees efficient transport of H(2)O(2) across the endoplasmic reticulum membrane
title_sort human aquaporin-11 guarantees efficient transport of h(2)o(2) across the endoplasmic reticulum membrane
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6812059/
https://www.ncbi.nlm.nih.gov/pubmed/31546170
http://dx.doi.org/10.1016/j.redox.2019.101326
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