Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation.

Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Research Abstract Details 

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Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Abstract Text:

K M Lindsey Rose,Z Wang,G N Magrath,E S Hazard,J D Hildebrandt,K L Schey,K M Lindsey Rose,Z Wang,G N Magrath,E S Hazard,J D Hildebrandt,K L Schey,

Aquaporin 0 (AQP0), also known as major intrinsic protein of lens, is the most abundant membrane protein in the lens and it undergoes a host of C-terminally directed posttranslational modifications. The C-terminal region containing the major phosphorylation sites is a putative calmodulin-binding site, and calmodulin has been shown to regulate AQP0 water permeability. The purpose of the present study was to elucidate the role of AQP0 phosphorylation on calmodulin binding. AQP0 C-terminal peptides were synthesized with and without serine phosphorylation on S231 and S235, and the ability of these peptides to bind dansyl-labeled calmodulin and the calcium dependence of the interaction was assessed using a fluorescence binding assay. The AQP0 C-terminal phosphorylated peptides were found to have 20-50-fold lower affinities for calmodulin than the unphosphorylated peptide. Chemical cross-linking studies revealed specific sites of AQP0-calmodulin interaction that are significantly reduced by AQP0 phosphorylation. These data suggest that AQP0 C-terminal phosphorylation affects calmodulin binding in vivo and has a role in regulation of AQP0 function.

Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Publishing Authors By Initials

KM Rose,Z Wang,GN Magrath,ES Hazard,JD Hildebrandt,KL Schey,KM Rose,Z Wang,GN Magrath,ES Hazard,JD Hildebrandt,KL Schey,

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Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biochemistry

VOLUME: 47

Page Numbers: 339-47

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 15

MONTH: 12

YEAR: 2007

Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation.

AFFILIATION: Department of Cell and Molecular Pharmacology, 173 Ashley Avenue, Medical University of South Carolina, Charleston, South Carolina 29425.

Country: United States

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MEDLINETA: Biochemistry

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