| First Author | Yakata K | Year | 2007 |
| Journal | Biochim Biophys Acta | Volume | 1768 |
| Issue | 3 | Pages | 688-93 |
| PubMed ID | 17178102 | Mgi Jnum | J:188552 |
| Mgi Id | MGI:5441073 | Doi | 10.1016/j.bbamem.2006.11.005 |
| Citation | Yakata K, et al. (2007) Aquaporin-11 containing a divergent NPA motif has normal water channel activity. Biochim Biophys Acta 1768(3):688-93 |
| abstractText | 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+/-0.03x10(-13) cm(3)/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels. |
