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  Argiotoxin detects molecular differences in AMPA receptor channels

Herlitze, S., Raditsch, M., Ruppersberg, J. P., Jahn, W., Monyer, H., Schöpfer, R., et al. (1993). Argiotoxin detects molecular differences in AMPA receptor channels. Neuron, 10(6), 1131-1140. doi:10.1016/0896-6273(93)90061-U.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AA46-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-274A-B
Genre: Journal Article

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Neuron_10_1993_1131.pdf (Any fulltext), 947KB
 
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 Creators:
Herlitze, Stefan1, Author           
Raditsch, Martin1, Author           
Ruppersberg, J. Peter1, Author           
Jahn, Werner2, 3, Author           
Monyer, Hannah4, Author           
Schöpfer, Ralf4, Author           
Witzemann, Veit1, 4, 5, 6, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              
4Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
5Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
6Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              

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 Abstract: Argiotoxin, a component of the spider venom from Argiope lobata, blocks AMPA receptor channels expressed in homomeric and heteromeric configuration in Xenopus oocytes. Argiotoxin acts as an open channel blocker in a voltage-dependent manner and discriminates between the functionally diverse AMPA receptors. Importantly, a transmembrane region 2 determinant for divalent cation permeability also determines argiotoxin sensitivity. Subunit-specific differences in the time courses of block and recovery demonstrate that heteromeric AMPA receptors can assemble in variable ratios. Thus, argiotoxin can be used as a tool in analyzing the subunit composition of AMPA receptors in native membranes.

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Language(s): eng - English
 Dates: 1993-06
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666828
DOI: 10.1016/0896-6273(93)90061-U
URI: https://www.ncbi.nlm.nih.gov/pubmed/7686380
 Degree: -

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Title: Neuron
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 10 (6) Sequence Number: - Start / End Page: 1131 - 1140 Identifier: ISSN: 0896-6273
CoNE: https://pure.mpg.de/cone/journals/resource/954925560565