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

Journal of Structural and Functional Genomics
Nadezda V KovalevskayaGeerten W Vuister

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.

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Citations

Oct 2, 2012·Journal of the American Society of Nephrology : JASN·Kukiat TudporJoost G J Hoenderop
Apr 24, 2013·Pflügers Archiv : European journal of physiology·Nadezda V KovalevskayaGeerten W Vuister
Apr 25, 2018·International Journal of Molecular Sciences·Raquibul Hasan, Xuming Zhang
Jun 12, 2019·Channels·Ana Elena López-RomeroTamara Rosenbaum
Feb 20, 2020·The Journal of Physiology·Maria V YelshanskayaAlexander I Sobolevsky
May 24, 2017·Pflügers Archiv : European journal of physiology·Mark K van GoorJenny van der Wijst
Aug 18, 2018·Science Advances·Appu K SinghAlexander I Sobolevsky
Mar 27, 2019·Cold Spring Harbor Perspectives in Biology·Laura Vangeel, Thomas Voets
Aug 31, 2021·The Journal of Biological Chemistry·Mahnaz AminiAndreas Beck

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Methods Mentioned

BETA
NMR
Fluorescence
pull-down
fluorescence spectroscopy

Software Mentioned

CcpNmr Analysis
NMRpipe suite
Origin

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