Aquaporin 6 binds calmodulin in a calcium-dependent manner.

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Rabaud, NE; Song, L; Wang, Y; Agre, P; Yasui, M; Carbrey, JM

Published Date

  • May 22, 2009

Published In

Volume / Issue

  • 383 / 1

Start / End Page

  • 54 - 57

PubMed ID

  • 19336226

Electronic International Standard Serial Number (EISSN)

  • 1090-2104

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2009.03.128

Language

  • eng

Conference Location

  • United States