Aquaporin 6 binds calmodulin in a calcium-dependent manner

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

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)54-57
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume383
Issue number1
DOIs
Publication statusPublished - 2009 May 22

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Keywords

  • AQP6
  • Aquaporin
  • Calcium
  • Calmodulin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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