English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

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

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.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-7FAC-E Version Permalink: http://hdl.handle.net/21.11116/0000-0001-3F43-E
Genre: Journal Article

Files

show Files
hide Files
:
2457108.pdf (Publisher version), 3MB
Name:
2457108.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
2457108_Suppl_1.htm (Supplementary material), 213KB
Name:
2457108_Suppl_1.htm
Description:
-
Visibility:
Public
MIME-Type / Checksum:
text/html / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2457108_Suppl_2.docx (Supplementary material), 23KB
Name:
2457108_Suppl_2.docx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.wordprocessingml.document / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2457108_Suppl_3.docx (Supplementary material), 25KB
Name:
2457108_Suppl_3.docx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.wordprocessingml.document / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2457108_Suppl_4.jpeg (Supplementary material), 114KB
Name:
2457108_Suppl_4.jpeg
Description:
-
Visibility:
Public
MIME-Type / Checksum:
image/jpeg / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Picher, M. M.1, Author              
Oprişoreanu, A. M., Author
Jung, S.1, Author              
Michel, K., Author
Schoch, S., Author
Moser, T.1, Author              
Affiliations:
1Research Group of Synaptic Nanophysiology, MPI for Biophysical Chemistry, Max Planck Society, ou_2205655              

Content

show
hide
Free keywords: active zone, ribbon synapse, hair cell, channel clustering, exocytosis, hearing
 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.

Details

show
hide
Language(s): eng - English
 Dates: 2017-06-08
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.3389/fncel.2017.00160
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Frontiers in Cellular Neuroscience
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 11 Volume / Issue: 11 Sequence Number: 160 Start / End Page: 160-1 - 160-11 Identifier: -