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J Struct Funct Genomics. 2012 Jun;13(2):91-100. doi: 10.1007/s10969-012-9128-4. Epub 2012 Feb 22.

The TRPV5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties.

Author information

1
Department of Protein Biophysics, IMM, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands. n.kovalevskaya@science.ru.nl

Abstract

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.

PMID:
22354706
PMCID:
PMC3375010
DOI:
10.1007/s10969-012-9128-4
[Indexed for MEDLINE]
Free PMC Article

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