The KA-2 subunit of excitatory amino acid receptors shows widespread expression 
in brain and forms ion channels with distantly related subunits

Herb, Anne; Burnashev, Nail; Werner, Pia; Sakmann, Bert; Wisden, William; Seeburg, Peter H.

doi:10.1016/0896-6273(92)90098-X

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The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits

Herb, A., Burnashev, N., Werner, P., Sakmann, B., Wisden, W., & Seeburg, P. H. (1992). The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits. Neuron, 8, 775-785. doi:10.1016/0896-6273(92)90098-X.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AC34-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0002-60B6-4

Genre: Journal Article

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https://www.sciencedirect.com/science/article/pii/089662739290098X/pdf?md5=78e8036410a1a206d548463d1276cb40&pid=1-s2.0-089662739290098X-main.pdf (Any fulltext) Open Access status unknown

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Creators:
Herb, Anne¹, Author
Burnashev, Nail², Author
Werner, Pia¹, Author
Sakmann, Bert², Author
Wisden, William, Author
Seeburg, Peter H.¹, Author

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1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701

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Abstract: A new ionotropic glutamate receptor subunit termed KA-2, cloned from rat brain cDNA, exhibits high affinity for [3H]kainate (KD approximately 15 nM). KA-2 mRNA is widely expressed in embryonic and adult brain. Homomeric KA-2 expression does not generate agonist-sensitive channels, but currents are observed when KA-2 is coexpressed with GluR5 or GluR6 subunits. Specifically, coexpression of GluR5(R) and KA-2 produces channel activity, whereas homomeric expression of either subunit does not. Currents through heteromeric GluR5(Q)/KA-2 channels show more rapid desensitization and different current-voltage relations when compared with GluR5(Q) currents. GluR6/KA-2 channels are gated by AMPA, which fails to gate homomeric GluR6 receptor channels. These results suggest possible in vivo partnership relations for high affinity kainate receptors.

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Language(s): eng - English

Dates: Modified: 1992-01-21Submitted: 1991-12-09Published Online: 2004-09-07Date issued: 1992-04-01

Publication Status: Issued

Pages: 11

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Rev. Type: Peer

Identifiers: DOI: 10.1016/0896-6273(92)90098-X
URI: https://www.ncbi.nlm.nih.gov/pubmed/1373632
URI: http://www.cell.com/neuron/fulltext/0896-6273(92)90098-X

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Title: Neuron

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Publ. Info: Cambridge, Mass. : Cell Press

Pages: - Volume / Issue: 8 Sequence Number: - Start / End Page: 775 - 785 Identifier: ISSN: 0896-6273
CoNE: https://pure.mpg.de/cone/journals/resource/954925560565