抄録
Aquaporin 6 (AQP6) is an anion channel that is expressed primarily in acid secreting α-intercalated cells of the kidney collecting duct. In addition, AQP6 anion channel permeability is gated by low pH. Inspection of the N-terminus of AQP6 revealed a putative calmodulin binding site. AQP6-expressing CHO-K1 cell lysates were mixed with calmodulin beads and AQP6 was pulled down in the presence of calcium. Mutagenesis of the N-terminal calmodulin binding site in full length mouse AQP6 resulted in a loss of calmodulin binding activity. Mouse and human AQP6 calmodulin binding site peptides bound dansyl-calmodulin with a dissociation constant of approximately 1 μM. The binding of AQP6 to calmodulin may be an important key to determining the physiological role of AQP6 in the kidney.
| 元の言語 | English |
|---|---|
| ページ（範囲） | 54-57 |
| ページ数 | 4 |
| ジャーナル | Biochemical and Biophysical Research Communications |
| 巻 | 383 |
| 発行部数 | 1 |
| DOI | |
| 出版物ステータス | Published - 2009 5 22 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
これを引用
Aquaporin 6 binds calmodulin in a calcium-dependent manner. / Rabaud, Nicole E.; Song, Linhua; Wang, Yiding; Agre, Peter; Yasui, Masato; Carbrey, Jennifer M.
：: Biochemical and Biophysical Research Communications, 巻 383, 番号 1, 22.05.2009, p. 54-57.研究成果: Article
}
TY - JOUR
T1 - Aquaporin 6 binds calmodulin in a calcium-dependent manner
AU - Rabaud, Nicole E.
AU - Song, Linhua
AU - Wang, Yiding
AU - Agre, Peter
AU - Yasui, Masato
AU - Carbrey, Jennifer M.
PY - 2009/5/22
Y1 - 2009/5/22
N2 - Aquaporin 6 (AQP6) is an anion channel that is expressed primarily in acid secreting α-intercalated cells of the kidney collecting duct. In addition, AQP6 anion channel permeability is gated by low pH. Inspection of the N-terminus of AQP6 revealed a putative calmodulin binding site. AQP6-expressing CHO-K1 cell lysates were mixed with calmodulin beads and AQP6 was pulled down in the presence of calcium. Mutagenesis of the N-terminal calmodulin binding site in full length mouse AQP6 resulted in a loss of calmodulin binding activity. Mouse and human AQP6 calmodulin binding site peptides bound dansyl-calmodulin with a dissociation constant of approximately 1 μM. The binding of AQP6 to calmodulin may be an important key to determining the physiological role of AQP6 in the kidney.
AB - Aquaporin 6 (AQP6) is an anion channel that is expressed primarily in acid secreting α-intercalated cells of the kidney collecting duct. In addition, AQP6 anion channel permeability is gated by low pH. Inspection of the N-terminus of AQP6 revealed a putative calmodulin binding site. AQP6-expressing CHO-K1 cell lysates were mixed with calmodulin beads and AQP6 was pulled down in the presence of calcium. Mutagenesis of the N-terminal calmodulin binding site in full length mouse AQP6 resulted in a loss of calmodulin binding activity. Mouse and human AQP6 calmodulin binding site peptides bound dansyl-calmodulin with a dissociation constant of approximately 1 μM. The binding of AQP6 to calmodulin may be an important key to determining the physiological role of AQP6 in the kidney.
KW - AQP6
KW - Aquaporin
KW - Calcium
KW - Calmodulin
UR - http://www.scopus.com/inward/record.url?scp=64949201126&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=64949201126&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2009.03.128
DO - 10.1016/j.bbrc.2009.03.128
M3 - Article
C2 - 19336226
AN - SCOPUS:64949201126
VL - 383
SP - 54
EP - 57
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -