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Journal Article

Ca2+-binding protein 2 inhibits Ca2+-channel inactivation in mouse inner hair cells.

MPS-Authors
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Picher,  M. M.
Research Group of Synaptic Nanophysiology, MPI for Biophysical Chemistry, Max Planck Society;

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Jung,  S.
Research Group of Synaptic Nanophysiology, MPI for Biophysical Chemistry, Max Planck Society;

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Moser,  T.
Research Group of Synaptic Nanophysiology, MPI for Biophysical Chemistry, Max Planck Society;

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Supplementary Material (public)

2395463_Suppl.DCSupplemental
(Supplementary material), 41KB

Citation

Picher, M. M., Gehrt, A., Meese, S., Ivanovic, A., Predoehl, F., Jung, S., et al. (2017). Ca2+-binding protein 2 inhibits Ca2+-channel inactivation in mouse inner hair cells. Proceedings of the National Academy of Sciences of the United States of America, 114(9), E1717-E1726. doi:10.1073/pnas.1617533114.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-62F8-C
Abstract
Ca2+ channels mediate excitation-secretion coupling and show little inactivation at sensory ribbon synapses, enabling reliable synaptic information transfer during sustained stimulation. Studies of Ca2+-channel complexes in HEK293 cells indicated that Ca2+-binding proteins (CaBPs) antagonize their calmodulin-dependent inactivation. Although human mutations affecting CABP2 were shown to cause hearing impairment, the role of CaBP2 in auditory function and the precise disease mechanism remained enigmatic. Here, we disrupted CaBP2 in mice and showed that CaBP2 is required for sound encoding at inner hair cell synapses, likely by suppressing Ca2+-channel inactivation. We propose that the number of activatable Ca2+ channels at the active zone is reduced when CaBP2 is lacking, as is likely the case with the newly described human CABP2 mutation.