| Literature DB >> 19336226 |
Nicole E Rabaud1, Linhua Song, Yiding Wang, Peter Agre, Masato Yasui, Jennifer M Carbrey.
Abstract
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.Entities:
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Year: 2009 PMID： 19336226 PMCID： PMC2695410 DOI： 10.1016/j.bbrc.2009.03.128
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575