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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Bibliographic Details
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
Description
Summary: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.
ISSN:2211-5463

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