University of Leicester
Browse
The TRPV5?6 calcium channels contain multiple calmodulin binding sites with differential binding properties..pdf (4.46 MB)

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

Download (4.46 MB)
journal contribution
posted on 2012-10-24, 09:22 authored by NV Kovalevskaya, FM Bokhovchuk, GW Vuister
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.

Funding

Netherlands Organization for Scientific Research (700.55.443 and 700.57.101)

History

Citation

J Struct Funct Genomics, 2012, 13 (2), pp. 91-100

Author affiliation

Molecular & Cell Biology

Version

  • VoR (Version of Record)

Published in

Journal of Structural and Functional Genomics

Volume

13

Issue

2

Pagination

91–100

Publisher

Springer Verlag

eissn

1570-0267

Acceptance date

2012-02-02

Copyright date

2012

Available date

2012-02-22

Language

eng

Publisher version

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3375010/