GABAB receptor constituents revealed by tandem affinity purification from transgenic mice.

Tudor Bartoi; Kristoffer T G Rigbolt; Dan Du; Georg Köhr; Blagoy Blagoev; Hans-Christian Kornau

GABAB receptor constituents revealed by tandem affinity purification from transgenic mice.

Standard

GABAB receptor constituents revealed by tandem affinity purification from transgenic mice. / Bartoi, Tudor; Rigbolt, Kristoffer T G; Du, Dan; Köhr, Georg; Blagoev, Blagoy; Kornau, Hans-Christian.

in: J BIOL CHEM, Jahrgang 285, Nr. 27, 27, 2010, S. 20625-20633.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Bartoi, T, Rigbolt, KTG, Du, D, Köhr, G, Blagoev, B & Kornau, H-C 2010, 'GABAB receptor constituents revealed by tandem affinity purification from transgenic mice.', J BIOL CHEM, Jg. 285, Nr. 27, 27, S. 20625-20633. <http://www.ncbi.nlm.nih.gov/pubmed/20406808?dopt=Citation>

APA

Bartoi, T., Rigbolt, K. T. G., Du, D., Köhr, G., Blagoev, B., & Kornau, H-C. (2010). GABAB receptor constituents revealed by tandem affinity purification from transgenic mice. J BIOL CHEM, 285(27), 20625-20633. [27]. http://www.ncbi.nlm.nih.gov/pubmed/20406808?dopt=Citation

Vancouver

Bartoi T, Rigbolt KTG, Du D, Köhr G, Blagoev B, Kornau H-C. GABAB receptor constituents revealed by tandem affinity purification from transgenic mice. J BIOL CHEM. 2010;285(27):20625-20633. 27.

Bibtex

@article{05d1ed0f5d3f49fc93d2c23d80eeaa3a,

title = "GABAB receptor constituents revealed by tandem affinity purification from transgenic mice.",

abstract = "GABA(B) receptors function as heterodimeric G-protein-coupled receptors for the neurotransmitter gamma-aminobutyric acid (GABA). Receptor subtypes, based on isoforms of the ligand-binding subunit GABA(B1), are thought to involve a differential set of associated proteins. Here, we describe two mouse lines that allow a straightforward biochemical isolation of GABA(B) receptors. The transgenic mice express GABA(B1) 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 GABA(B1) complex. One of the identified proteins, potassium channel tetramerization domain-containing protein 12, associates with heterodimeric GABA(B) receptors via the GABA(B2) subunit. In transfected hippocampal neurons, potassium channel tetramerization domain-containing protein 12 augmented axonal surface targeting of GABA(B2). The mice equipped with tags on GABA(B1) facilitate validation and identification of native binding partners of GABA(B) receptors, providing insight into the molecular mechanisms of synaptic modulation.",

keywords = "Animals, Brain physiology, Gene Expression Regulation, Mice, CHO Cells, Cricetinae, Cricetulus, Rats, Exons genetics, Green Fluorescent Proteins genetics, Mice, Transgenic, Neurons physiology, In Situ Hybridization, Blotting, Western, Transfection, Aequorin genetics, Chromosomes, Artificial, Bacterial genetics, Cloning, Molecular, Genes, Reporter, Receptors, GABA-B genetics, Animals, Brain physiology, Gene Expression Regulation, Mice, CHO Cells, Cricetinae, Cricetulus, Rats, Exons genetics, Green Fluorescent Proteins genetics, Mice, Transgenic, Neurons physiology, In Situ Hybridization, Blotting, Western, Transfection, Aequorin genetics, Chromosomes, Artificial, Bacterial genetics, Cloning, Molecular, Genes, Reporter, Receptors, GABA-B genetics",

author = "Tudor Bartoi and Rigbolt, {Kristoffer T G} and Dan Du and Georg K{\"o}hr and Blagoy Blagoev and Hans-Christian Kornau",

year = "2010",

language = "Deutsch",

volume = "285",

pages = "20625--20633",

journal = "J BIOL CHEM",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "27",

}

RIS

TY - JOUR

T1 - GABAB receptor constituents revealed by tandem affinity purification from transgenic mice.

AU - Bartoi, Tudor

AU - Rigbolt, Kristoffer T G

AU - Du, Dan

AU - Köhr, Georg

AU - Blagoev, Blagoy

AU - Kornau, Hans-Christian

PY - 2010

Y1 - 2010

N2 - GABA(B) receptors function as heterodimeric G-protein-coupled receptors for the neurotransmitter gamma-aminobutyric acid (GABA). Receptor subtypes, based on isoforms of the ligand-binding subunit GABA(B1), are thought to involve a differential set of associated proteins. Here, we describe two mouse lines that allow a straightforward biochemical isolation of GABA(B) receptors. The transgenic mice express GABA(B1) 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 GABA(B1) complex. One of the identified proteins, potassium channel tetramerization domain-containing protein 12, associates with heterodimeric GABA(B) receptors via the GABA(B2) subunit. In transfected hippocampal neurons, potassium channel tetramerization domain-containing protein 12 augmented axonal surface targeting of GABA(B2). The mice equipped with tags on GABA(B1) facilitate validation and identification of native binding partners of GABA(B) receptors, providing insight into the molecular mechanisms of synaptic modulation.

AB - GABA(B) receptors function as heterodimeric G-protein-coupled receptors for the neurotransmitter gamma-aminobutyric acid (GABA). Receptor subtypes, based on isoforms of the ligand-binding subunit GABA(B1), are thought to involve a differential set of associated proteins. Here, we describe two mouse lines that allow a straightforward biochemical isolation of GABA(B) receptors. The transgenic mice express GABA(B1) 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 GABA(B1) complex. One of the identified proteins, potassium channel tetramerization domain-containing protein 12, associates with heterodimeric GABA(B) receptors via the GABA(B2) subunit. In transfected hippocampal neurons, potassium channel tetramerization domain-containing protein 12 augmented axonal surface targeting of GABA(B2). The mice equipped with tags on GABA(B1) facilitate validation and identification of native binding partners of GABA(B) receptors, providing insight into the molecular mechanisms of synaptic modulation.

KW - Animals

KW - Brain physiology

KW - Gene Expression Regulation

KW - Mice

KW - CHO Cells

KW - Cricetinae

KW - Cricetulus

KW - Rats

KW - Exons genetics

KW - Green Fluorescent Proteins genetics

KW - Mice, Transgenic

KW - Neurons physiology

KW - In Situ Hybridization

KW - Blotting, Western

KW - Transfection

KW - Aequorin genetics

KW - Chromosomes, Artificial, Bacterial genetics

KW - Cloning, Molecular

KW - Genes, Reporter

KW - Receptors, GABA-B genetics

KW - Animals

KW - Brain physiology

KW - Gene Expression Regulation

KW - Mice

KW - CHO Cells

KW - Cricetinae

KW - Cricetulus

KW - Rats

KW - Exons genetics

KW - Green Fluorescent Proteins genetics

KW - Mice, Transgenic

KW - Neurons physiology

KW - In Situ Hybridization

KW - Blotting, Western

KW - Transfection

KW - Aequorin genetics

KW - Chromosomes, Artificial, Bacterial genetics

KW - Cloning, Molecular

KW - Genes, Reporter

KW - Receptors, GABA-B genetics

M3 - SCORING: Zeitschriftenaufsatz

VL - 285

SP - 20625

EP - 20633

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 27

M1 - 27

ER -