Dalamon, VivianaFiori, MarianaFigueroa, VaniaOliva, CarolinaDel Río, RodrigoGonzález, WendyCanan, JonathanElgoyhen, AnaAltenberg, GuillermoRetamal, Mauricio2017-01-032017-01-032016Dalamon V, Fiori MC, Figueroa VA, Oliva CA, Del Rio R, Gonzalez W, Canan J, Elgoyhen AB, Altenberg GA, Retamal MA. Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness. Pflugers Arch. 2016 May;468(5):909-18.http://hdl.handle.net/11447/912http://dx.doi.org/ 10.1007/s00424-016-1788-7Centro de Fisiología Celular e IntegrativaGap-junction channels (GJCs) are formed by head-to-head association of two hemichannels (HCs, connexin hexamers). HCs and GJCs are permeable to ions and hydrophilic molecules of up to Mr ~1 kDa. Hearing impairment of genetic origin is common, and mutations of connexin 26 (Cx26) are its major cause. We recently identified two novel Cx26 mutations in hearing-impaired subjects, L10P and G109V. L10P forms functional GJCs with slightly altered voltage dependence and HCs with decrease ATP/cationic dye selectivity. G109V does not form functional GJCs, but forms functional HCs with enhanced extracellular Ca2+ sensitivity and subtle alterations in voltage dependence and ATP/cationic dye selectivity. Deafness associated with G109V could result from decreased GJCs activity, whereas deafness associated to L10P may have a more complex mechanism that involves changes in HC permeability.en-USDeafnessHemichannelsConnexinsGap-junction channelsIon channelMutationArtículo