The TRPV5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties.
SourceJournal of Structural and Functional Genomics, 13, 2, (2012), pp. 91-100
1 juni 2012
Article / Letter to editor
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Journal of Structural and Functional Genomics
SubjectBio-Organic Chemistry; Biophysical Chemistry; NCMLS 5: Membrane transport and intracellular motility IGMD 9: Renal disorder
The epithelial Ca(2+) channels TRPV5/6 (transient receptor potential vanilloid 5/6) are thoroughly regulated in order to fine-tune the amount of Ca(2+) reabsorption. Calmodulin has been shown to be involved into calcium-dependent inactivation of TRPV5/6 channels by binding directly to the distal C-terminal fragment of the channels (de Groot et al. in Mol Cell Biol 31:2845-2853, 12). Here, we investigate this binding in detail and find significant differences between TRPV5 and TRPV6. We also identify and characterize in vitro four other CaM binding fragments of TRPV5/6, which likely are also involved in TRPV5/6 channel regulation. The five CaM binding sites display diversity in binding modes, binding stoichiometries and binding affinities, which may fine-tune the response of the channels to varying Ca(2+)-concentrations.
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