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.
本文言語 | 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 |
号 | 1 |
DOI | |
出版ステータス | Published - 2009 5月 22 |
ASJC Scopus subject areas
- 生物理学
- 生化学
- 分子生物学
- 細胞生物学