Aquaporin 6 binds calmodulin in a calcium-dependent manner

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

doi:10.1016/j.bbrc.2009.03.128

Aquaporin 6 binds calmodulin in a calcium-dependent manner

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

Department of Pharmacology

Research output: Contribution to journal › Article › peer-review

22 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 language	English
Pages (from-to)	54-57
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	383
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2009.03.128
Publication status	Published - 2009 May 22

Keywords

AQP6
Aquaporin
Calcium
Calmodulin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2009.03.128

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title = "Aquaporin 6 binds calmodulin in a calcium-dependent manner",

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.",

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author = "Rabaud, {Nicole E.} and Linhua Song and Yiding Wang and Peter Agre and Masato Yasui and Carbrey, {Jennifer M.}",

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AU - Song, Linhua

AU - Wang, Yiding

AU - Agre, Peter

AU - Yasui, Masato

AU - Carbrey, Jennifer M.

N1 - Funding Information: This work was supported in part by National Institutes of Health Grant DK065098.

PY - 2009/5/22

Y1 - 2009/5/22

N2 - 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.

AB - 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.

KW - AQP6

KW - Aquaporin

KW - Calcium

KW - Calmodulin

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Aquaporin 6 binds calmodulin in a calcium-dependent manner

Abstract

Keywords

ASJC Scopus subject areas

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