Argiotoxin detects molecular differences in AMPA receptor channels

Herlitze, Stefan; Raditsch, Martin; Ruppersberg, J. Peter; Jahn, Werner; Monyer, Hannah; Schöpfer, Ralf; Witzemann, Veit

doi:10.1016/0896-6273(93)90061-U

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Argiotoxin detects molecular differences in AMPA receptor channels

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Herlitze, Stefan
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Raditsch, Martin
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Ruppersberg, J. Peter
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Jahn, Werner
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Monyer, Hannah
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Schöpfer, Ralf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Witzemann, Veit
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/089662739390061U/pdf?md5=a26cdcd7890c623d3e8a7b363b30c1c9&pid=1-s2.0-089662739390061U-main.pdf
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Zitation

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.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-AA46-2

Zusammenfassung

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.