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

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 Cys227 causes renal failure. However the importance of Cys227 for the molecular function of AQP11 is largely unknown. In this study, we examined...

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Main Authors: Saki Takahashi, Kanako Muta, Hiroko Sonoda, Ayaka Kato, Ahmed Abdeen, Masahiro Ikeda
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:FEBS Open Bio
Subjects:
Aqauaporin-11
Water channel
Water permeability
Online Access:http://www.sciencedirect.com/science/article/pii/S221154631400028X
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spelling doaj-aec8f57f428a4437939c927ae908c9462020-11-25T03:55:11ZengWileyFEBS Open Bio2211-54632014-01-014C31532010.1016/j.fob.2014.03.005The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11Saki TakahashiKanako MutaHiroko SonodaAyaka KatoAhmed AbdeenMasahiro IkedaAquaporin-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 Cys227 causes renal failure. However the importance of Cys227 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 Cys227. 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 Cys227 is crucial for the proper molecular function of AQP11.http://www.sciencedirect.com/science/article/pii/S221154631400028XAqauaporin-11Water channelWater permeability
collection DOAJ
language English
format Article
sources DOAJ
author Saki Takahashi
Kanako Muta
Hiroko Sonoda
Ayaka Kato
Ahmed Abdeen
Masahiro Ikeda
spellingShingle Saki Takahashi
Kanako Muta
Hiroko Sonoda
Ayaka Kato
Ahmed Abdeen
Masahiro Ikeda
The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
FEBS Open Bio
Aqauaporin-11
Water channel
Water permeability
author_facet Saki Takahashi
Kanako Muta
Hiroko Sonoda
Ayaka Kato
Ahmed Abdeen
Masahiro Ikeda
author_sort Saki Takahashi
title 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_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_sort role of cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11
publisher Wiley
series FEBS Open Bio
issn 2211-5463
publishDate 2014-01-01
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 Cys227 causes renal failure. However the importance of Cys227 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 Cys227. 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 Cys227 is crucial for the proper molecular function of AQP11.
topic Aqauaporin-11
Water channel
Water permeability
url http://www.sciencedirect.com/science/article/pii/S221154631400028X
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