
Aquaporin 6 binds calmodulin in a calcium-dependent manner.
Aquaporin 6 (AQP6) is an anion channel that is expressed primarily in acid secreting alpha-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 1microM. The binding of AQP6 to calmodulin may be an important key to determining the physiological role of AQP6 in the kidney.
Duke Scholars
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Related Subject Headings
- Rats
- Protein Structure, Tertiary
- Protein Binding
- Molecular Sequence Data
- Mice
- Humans
- Cricetulus
- Cricetinae
- Calmodulin
- Calcium
Citation

Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Rats
- Protein Structure, Tertiary
- Protein Binding
- Molecular Sequence Data
- Mice
- Humans
- Cricetulus
- Cricetinae
- Calmodulin
- Calcium