2. Academic Validation
  3. 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

  • FEBS Open Bio. 2014 Mar 18;4:315-20. doi: 10.1016/j.fob.2014.03.005.
Saki Takahashi 1,  Kanako Muta 1,  Hiroko Sonoda 1,  Ayaka Kato 1,  Ahmed Abdeen 1,  Masahiro Ikeda 1
Affiliations

Affiliation

  • 1 Department of Veterinary Pharmacology, University of Miyazaki, Miyazaki 889-2192, Japan.
PMID: 24918044 DOI: 10.1016/j.fob.2014.03.005
Abstract

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.

Keywords

AQP, aquaporin; Aqauaporin-11; DsRM, DsRed-Monomer; ER, endoplasmic reticulum; GFP, green fluorescent protein; Water channel; Water permeability.

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