| First Author | Rabaud NE | Year | 2009 |
| Journal | Biochem Biophys Res Commun | Volume | 383 |
| Issue | 1 | Pages | 54-7 |
| PubMed ID | 19336226 | Mgi Jnum | J:148347 |
| Mgi Id | MGI:3844389 | Doi | 10.1016/j.bbrc.2009.03.128 |
| Citation | Rabaud NE, et al. (2009) Aquaporin 6 binds calmodulin in a calcium-dependent manner. Biochem Biophys Res Commun 383(1):54-7 |
| abstractText | 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. |
