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  Multiple domains in the Kv7.3 C-terminus can regulate localization to the axon initial segment

Hefting, L. L., D´Este, E., Arvedsen, E., Benned-Jensen, T., & Rasmussen, H. B. (2020). Multiple domains in the Kv7.3 C-terminus can regulate localization to the axon initial segment. Frontiers in Cellular Neuroscience, 14: 10, pp. 1-17. doi:10.3389/fncel.2020.00010.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-A8F8-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-058A-9
Genre: Journal Article

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FrontCellNeurosci_14_2020_010.pdf (Any fulltext), 6MB
 
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 Creators:
Hefting, Louise Leth, Author
D´Este, Elisa1, Author              
Arvedsen, Emil, Author
Benned-Jensen, Tau, Author
Rasmussen, Hanne Borger, Author
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1Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society, ou_578627              

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Free keywords: ankyrin-G, hippocampal neurons, Kv7, KCNQ, FRAP, double-FRAP, STED, nanoscopy
 Abstract: The voltage-gated Kv7.2/Kv7.3 potassium channel is a critical regulator of neuronal excitability. It is strategically positioned at the axon initial segment (AIS) of neurons, where it effectively inhibits repetitive action potential firing. While the selective accumulation of Kv7.2/Kv7.3 channels at the AIS requires binding to the adaptor protein ankyrin G, it is currently unknown if additional molecular mechanisms contribute to the localization and fine-tuning of channel numbers at the AIS. Here, we utilized a chimeric approach to pinpoint regions within the Kv7.3 C-terminal tail with an impact upon AIS localization. This strategy identified two domains with opposing effects upon the AIS localization of Kv7.3 chimeras expressed in cultured hippocampal neurons. While a membrane proximal domain reduced AIS localization of Kv7.3 chimeras, helix D increased and stabilized chimera AIS localization. None of the identified domains were required for AIS localization. However, the domains modulated the relative efficiency of the localization raising the possibility that the two domains contribute to the regulation of Kv7 channel numbers and nanoscale organization at the AIS.

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Language(s): eng - English
 Dates: 2019-08-222020-01-142020-02-04
 Publication Status: Published online
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fncel.2020.00010
 Degree: -

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Title: Frontiers in Cellular Neuroscience
Source Genre: Journal
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Publ. Info: Lausanne : Frontiers Media
Pages: - Volume / Issue: 14 Sequence Number: 10 Start / End Page: 1 - 17 Identifier: ISSN: 1662-5102