1. Aquaporin-11 containing a divergent NPA motif has normal water channel activity
- Author
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Yakata, Kaya, Hiroaki, Yoko, Ishibashi, Kenichi, Sohara, Eisei, Sasaki, Sei, Mitsuoka, Kaoru, and Fujiyoshi, Yoshinori
- Subjects
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AQUAPORINS , *MEMBRANE proteins , *CHANNELS (Structural members) , *BILAYER lipid membranes - Abstract
Abstract: Recently, two novel mammalian aquaporins (AQPs), AQPs 11 and 12, have been identified and classified as members of a new AQP subfamily, the “subcellular AQPs”. In members of this subfamily one of the two asparagine–proline–alanine (NPA) motifs, which play a crucial role in selective water conduction, are not completely conserved. Mouse AQP11 (mAQP11) was expressed in Sf9 cells and purified using the detergent Fos-choline 10. The protein was reconstituted into liposomes, which were used for water conduction studies with a stopped-flow device. Single water permeability (pf) of AQP11 was measured to be 1.72±0.03×10−13 cm3/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels. [Copyright &y& Elsevier]
- Published
- 2007
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