Corrigendum to “Aquaporin-11 containing a divergent NPA motif has normal water channel activity” [Biochim. Biophys. Acta 1768 (2007) 688–693]
Corrigendum to “Aquaporin-11 containing a divergent NPA motif has normal water channel activity” [Biochim. Biophys. Acta 1768 (2007) 688–693]
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DOI:
10.1016/j.bbamem.2008.03.001
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发表时间:
2008-06
期刊:
影响因子:
--
通讯作者:
Kaya Yakata;Y. Hiroaki;K. Ishibashi;E. Sohara;S. Sasaki;K. Mitsuoka;Y. Fujiyoshi
中科院分区:
文献类型:
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作者:
Kaya Yakata;Y. Hiroaki;K. Ishibashi;E. Sohara;S. Sasaki;K. Mitsuoka;Y. Fujiyoshi
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±0.03×10−13cm3/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels.