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Rab interacting molecules 2 and 3 directly interact with the pore-forming CaV1.3 Ca2+ channel subunit and promote its membrane expression.

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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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2457108.pdf
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2457108_Suppl_1.htm
(Supplementary material), 213KB

2457108_Suppl_2.docx
(Supplementary material), 23KB

2457108_Suppl_3.docx
(Supplementary material), 25KB

2457108_Suppl_4.jpeg
(Supplementary material), 114KB

Citation

Picher, M. M., Oprişoreanu, A. M., Jung, S., Michel, K., Schoch, S., & Moser, T. (2017). Rab interacting molecules 2 and 3 directly interact with the pore-forming CaV1.3 Ca2+ channel subunit and promote its membrane expression. Frontiers in Cellular Neuroscience, 11: 160, pp. 160-1-160-11. doi:10.3389/fncel.2017.00160.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-7FAC-E
Abstract
Rab interacting molecules (RIMs) are multi-domain proteins that positively regulate the number of Ca2+ channels at the presynaptic active zone (AZ). Several molecular mechanisms have been demonstrated for RIM-binding to components of the presynaptic Ca2+ channel complex, the key signaling element at the AZ. Here, we report an interaction of the C2B domain of RIM2α and RIM3γ with the C-terminus of the pore-forming α–subunit of CaV1.3 channels (CaV1.3α1), which mediate stimulus-secretion coupling at the ribbon synapses of cochlear inner hair cells (IHCs). Co-expressing full-length RIM2α with a Ca2+ channel complex closely resembling that of IHCs (CaV1.3α1-CaVß2a) in HEK293 cells doubled the Ca2+-current and shifted the voltage-dependence of Ca2+ channel activation by approximately +3 mV. Co-expression of the short RIM isoform RIM3γ increased the CaV1.3α1-CaVß2a-mediated Ca2+-influx in HEK293 cells, but disruption of RIM3γ in mice left Ca2+-influx in IHCs and hearing intact. In conclusion, we propose that RIM2α and RIM3γ directly interact with the C-terminus of the pore-forming subunit of CaV1.3 Ca2+ channels and positively regulate their plasma membrane expression in HEK293 cells.