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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Detalles Bibliográficos
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
Descripción
Sumario: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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