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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-62F8-C Version Permalink: http://hdl.handle.net/21.11116/0000-0001-3F3C-7
Genre: Journal Article

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 Creators:
Picher, M. M.1, Author              
Gehrt, A., Author
Meese, S., Author
Ivanovic, A., Author
Predoehl, F., Author
Jung, S.1, Author              
Schrauwen, I., Author
Dragonetti, A. G., Author
Colombo, R., Author
Van Camp, G., Author
Strenzke, N., Author
Moser, T.1, Author              
Affiliations:
1Research Group of Synaptic Nanophysiology, MPI for Biophysical Chemistry, Max Planck Society, ou_2205655              

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Free keywords: Ca2+ channel; inner hair cell; ribbon synapse; synaptopathy; hearing impairment
 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.

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Language(s): eng - English
 Dates: 2017-02-092017-02-28
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1617533114
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 114 (9) Sequence Number: - Start / End Page: E1717 - E1726 Identifier: -