Aquaporin 6 binds calmodulin in a calcium-dependent manner

Nicole E. Rabaud, Linhua Song, Yiding Wang, Peter Agre, Masato Yasui, Jennifer M. Carbrey

研究成果: Article査読

22 被引用数 (Scopus)

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
383
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

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