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

摘要

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^2^2^7 causes renal failure. However the importance of Cys^2^2^7 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^2^2^7. 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^2^2^7 is crucial for the proper molecular function of AQP11.