Open AccessThe role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin‐11
Author(s) -
Takahashi Saki,
Muta Kanako,
Sonoda Hiroko,
Kato Ayaka,
Abdeen Ahmed,
Ikeda Masahiro
Publication year - 2014
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2014.03.005
Subject(s) - aquaporin , subcellular localization , water channel , mutant , cysteine , mutation , microbiology and biotechnology , permeability (electromagnetism) , chemistry , hek 293 cells , function (biology) , aquaporin 1 , in vivo , biophysics , biology , biochemistry , genetics , gene , membrane , enzyme , mechanical engineering , engineering , inlet
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.