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Aquaporin-11 containing a divergent NPA motif has normal water channel activity |
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| Authors: | Kaya Yakata Kenichi Ishibashi Sei Sasaki Yoshinori Fujiyoshi |
| Institution: | a Department of Biophysics, Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku Kyoto 606-8502, Japan b Core Research for Evolution Science and Technology (CREST), Japan Science and Technology Agency (JST), Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan c Clinical Research Center, Chiba-East National Hospital, Chiba 260-8712, Japan d Department of Nephrology, Graduate School of Medicine, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo 113-8519, Japan e Japan Biological Information Research Center (JBIRC), The National Institute of Advanced Industrial Science and Technology (AIST), 2-41-6 Aomi, Koto-ku, Tokyo 135-0064, Japan |
| 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. |
| Keywords: | AQP aquaporin NPA motif asparagine-proline-alanine motif ER endoplasmic reticulum SIPs small basic intrinsic proteins DMPC dimyristoylphosphatidylcholine SuD single channel density |
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