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A persulfidation-based mechanism controls aquaporin-8 conductance

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dc.affiliation.dptoUC3M. Departamento de BioingenierĆ­aes
dc.affiliation.grupoinvUC3M. Grupo de InvestigaciĆ³n: Tissue Engineering and Regenerative Medicine (TERMeG)en
dc.contributor.authorBestetti, Stefano
dc.contributor.authorMedraƱo Fernandez, Iria
dc.contributor.authorGalli, Mauro
dc.contributor.authorGhitti, Michela
dc.contributor.authorBienert, Gerd P.
dc.contributor.authorMusco, Giovanna
dc.contributor.authorOrsi, Andrea
dc.contributor.authorRubartelli, Anna
dc.contributor.authorSitia, Roberto
dc.date.accessioned2024-01-09T10:48:52Z
dc.date.available2024-01-09T10:48:52Z
dc.date.issued2018-05-02
dc.description.abstractUpon engagement of tyrosine kinase receptors, nicotinamide adenine dinucleotide phosphate (NADPH)-oxidases release H2O2 in the extracellular space. We reported previously that aquaporin-8 (AQP8) transports H2O2 across the plasma membrane and is reversibly gated during cell stress, modulating signal strength and duration. We show that AQP8 gating is mediated by persulfidation of cysteine 53 (C53). Treatment with H2S is sufficient to block H2O2 entry in unstressed cells. Silencing cystathionine beta-synthase (CBS) prevents closure, suggesting that this enzyme is the main source of H2S. Molecular modeling indicates that C53 persulfidation displaces a nearby histidine located in the narrowest part of the channel. We propose that H2O2 molecules transported through AQP8 sulfenylate C53, making it susceptible to H2S produced by CBS. This mechanism tunes H2O2 transport and may control signaling and limit oxidative stress.en
dc.description.sponsorshipThis work was supported in part through grants from the Associazione Italiana Ricerca sul Cancro (IG 2016-18824 to R.S. and IG 2016-15434 to A.R.), the Fondazione Cariplo (2015-0591 to R.S.), the Ministero della Salute (PE-2011-02352286 to R.S. and RF-2013-02354880 to G.M.), the Telethon (GGP15059 to R.S.), and the "Cinque per mille"; (to A.R.). G.P.B. was supported by an Emmy Noether grant 1668/1-1 from the Deutsche Forschungsgemeinschaft.en
dc.format.extent10es
dc.format.mimetypeapplication/pdfen
dc.identifier.bibliographicCitationBestetti, S., MedraƱo-Fernandez, I., Galli, M., Ghitti, M., Bienert, G. P., Musco, G., Orsi, A., Rubartelli, A., & Sitia, R. (2018). A persulfidation-based mechanism controls aquaporin-8 conductance. Science Advances, 4(5).es
dc.identifier.doihttps://doi.org/10.1126/sciadv.aar5770
dc.identifier.issn2375-2548
dc.identifier.publicationfirstpage1es
dc.identifier.publicationissue5es
dc.identifier.publicationlastpage9es
dc.identifier.publicationtitleScience Advancesen
dc.identifier.publicationvolume4es
dc.identifier.urihttps://hdl.handle.net/10016/39178
dc.identifier.uxxiAR/0000026660
dc.language.isoengen
dc.publisherAmerican Association for the Advancement of Scienceen
dc.rightsĀ© 2018 The Authors.en
dc.rightsAtribuciĆ³n-NoComercial 3.0 EspaƱa*
dc.rights.accessRightsopen accessen
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/es/*
dc.titleA persulfidation-based mechanism controls aquaporin-8 conductanceen
dc.typeresearch articleen
dspace.entity.typePublication
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