The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11

Aquaporin-11 (AQP11) is the latest member of the mammalian water channel protein family to be described. Recent in vivo studies have shown that mutation at Cys(227) causes renal failure. However the importance of Cys(227) for the molecular function of AQP11 is largely unknown. In this study, we exam...

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Detalles Bibliográficos
Autores principales: Takahashi, Saki, Muta, Kanako, Sonoda, Hiroko, Kato, Ayaka, Abdeen, Ahmed, Ikeda, Masahiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4048847/
https://www.ncbi.nlm.nih.gov/pubmed/24918044
http://dx.doi.org/10.1016/j.fob.2014.03.005
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author Takahashi, Saki
Muta, Kanako
Sonoda, Hiroko
Kato, Ayaka
Abdeen, Ahmed
Ikeda, Masahiro
author_facet Takahashi, Saki
Muta, Kanako
Sonoda, Hiroko
Kato, Ayaka
Abdeen, Ahmed
Ikeda, Masahiro
author_sort Takahashi, Saki
collection PubMed
description Aquaporin-11 (AQP11) is the latest member of the mammalian water channel protein family to be described. Recent in vivo studies have shown that mutation at Cys(227) causes renal failure. However the importance of Cys(227) for the molecular function of AQP11 is largely unknown. In this study, we examined the subcellular localization, water permeability, and multimerization of AQP11 with a mutation at Cys(227). Interestingly, cells expressing the mutants had significantly higher osmotic water permeability. In contrast, the mutation lowered the cell surface expression and multimerization levels. Our observations suggest that Cys(227) is crucial for the proper molecular function of AQP11.
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spelling pubmed-40488472014-06-10 The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11 Takahashi, Saki Muta, Kanako Sonoda, Hiroko Kato, Ayaka Abdeen, Ahmed Ikeda, Masahiro FEBS Open Bio Article Aquaporin-11 (AQP11) is the latest member of the mammalian water channel protein family to be described. Recent in vivo studies have shown that mutation at Cys(227) causes renal failure. However the importance of Cys(227) for the molecular function of AQP11 is largely unknown. In this study, we examined the subcellular localization, water permeability, and multimerization of AQP11 with a mutation at Cys(227). Interestingly, cells expressing the mutants had significantly higher osmotic water permeability. In contrast, the mutation lowered the cell surface expression and multimerization levels. Our observations suggest that Cys(227) is crucial for the proper molecular function of AQP11. Elsevier 2014-03-18 /pmc/articles/PMC4048847/ /pubmed/24918044 http://dx.doi.org/10.1016/j.fob.2014.03.005 Text en © 2014 The Authors http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Takahashi, Saki
Muta, Kanako
Sonoda, Hiroko
Kato, Ayaka
Abdeen, Ahmed
Ikeda, Masahiro
The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title_full The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title_fullStr The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title_full_unstemmed The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title_short The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
title_sort role of cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4048847/
https://www.ncbi.nlm.nih.gov/pubmed/24918044
http://dx.doi.org/10.1016/j.fob.2014.03.005
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