Aquaporin-11 containing a divergent NPA motif has normal water channel activity
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説明
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.
収録刊行物
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- Biochimica et Biophysica Acta (BBA) - Biomembranes
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Biochimica et Biophysica Acta (BBA) - Biomembranes 1768 (3), 688-693, 2007-03
Elsevier BV
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キーワード
- Proline
- Fos-choline 10
- Amino Acid Motifs
- Molecular Sequence Data
- Biophysics
- Subcellular-aquaporin
- Spodoptera
- Aquaporins
- Transfection
- Biochemistry
- Mice
- Animals
- Amino Acid Sequence
- Baculovirus
- Cells, Cultured
- Alanine
- Water
- Cell Biology
- Stopped-flow
- Recombinant Proteins
- Asparagine–proline–alanine (NPA)-motif
- Liposomes
- Asparagine
- Baculoviridae