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  GabaB receptor constitutents revealed by tandem affinity purification from transgenic mice

Bartoi, T., Rigbolt, K. T. G., Du, D., Köhr, G., Blagoev, B., & Kornau, H. C. (2010). GabaB receptor constitutents revealed by tandem affinity purification from transgenic mice. The Journal of Biological Chemistry, 285(27), 20625-20633. doi:10.1074/jbc.M109.049700.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-5136-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-5137-3
Genre: Journal Article
Alternative Title : GabaB receptor constitutents revealed by tandem affinity purification from transgenic mice

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JBiolChem_285_2010_20625.pdf (Any fulltext), 4MB
 
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 Creators:
Bartoi, Tudor, Author
Rigbolt, Kristoffer T. G., Author
Du, Dan1, Author              
Köhr, Georg1, Author              
Blagoev, Blagoy, Author
Kornau, Hans Christian1, Author              
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1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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 Abstract: GABAB receptors function as heterodimeric G-protein-coupled receptors for the neurotransmitter γ-aminobutyric acid (GABA). Receptor subtypes, based on isoforms of the ligand-binding subunit GABAB1, are thought to involve a differential set of associated proteins. Here, we describe two mouse lines that allow a straightforward biochemical isolation of GABAB receptors. The transgenic mice express GABAB1 isoforms that contain sequences for a two-step affinity purification, in addition to their endogenous subunit repertoire. Comparative analyses of purified samples from the transgenic mice and wild-type control animals revealed two novel components of the GABAB1 complex. One of the identified proteins, potassium channel tetramerization domain-containing protein 12, associates with heterodimeric GABAB receptors via the GABAB2 subunit. In transfected hippocampal neurons, potassium channel tetramerization domain-containing protein 12 augmented axonal surface targeting of GABAB2. The mice equipped with tags on GABAB1 facilitate validation and identification of native binding partners of GABAB receptors, providing insight into the molecular mechanisms of synaptic modulation.

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Language(s): eng - English
 Dates: 2009-07-282010-04-202010-07-02
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 285 (27) Sequence Number: - Start / End Page: 20625 - 20633 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1