Heterodimerization is required for the formation of a functional GABAB receptor

@article{White1998HeterodimerizationIR,
  title={Heterodimerization is required for the formation of a functional GABAB receptor},
  author={Julia H. M. White and Alan Wise and Martin J. Main and Andrew Green and Neil J. Fraser and Graham H. Disney and Ashley A. Barnes and Piers C. Emson and Steven M. Foord and Fiona H Marshall},
  journal={Nature},
  year={1998},
  volume={396},
  pages={679-682}
}
GABA (γ-aminobutyric acid) is the main inhibitory neurotransmitter in the mammalian central nervous system, where it exerts its effects through ionotropic (GABAA/C) receptors to produce fast synaptic inhibition and metabotropic (GABAB) receptors to produce slow, prolonged inhibitory signals. The gene encoding a GABAB receptor (GABABR1) has been cloned; however, when expressed in mammalian cells this receptor is retained as an immature glycoprotein on intracellular membranes and exhibits low… Expand
Signal Transduction by GABAB Receptor Heterodimers
TLDR
The interdependent nature of the two subunits for receptor function makes the GABAB receptor a useful model to explore the larger significance of GPCR dimerization for G-protein activation. Expand
Identification of a GABAB Receptor Subunit, gb2, Required for Functional GABAB Receptor Activity*
TLDR
Characterization of the tissue distribution of each of the receptors by in situhybridization histochemistry in rat brain revealed co-localization of gb1 and gb2 transcripts in many brain regions, suggesting the hypothesis that gb 1 and gB2 may interact in vivo. Expand
Native GABAB receptors are heteromultimers with a family of auxiliary subunits
TLDR
It is shown by functional proteomics that GABAB receptors in the brain are high-molecular-mass complexes of GABAB1, GABAB2 and members of a subfamily of the KCTD (potassium channel tetramerization domain-containing) proteins, established as auxiliary subunits of GABAb receptors that determine the pharmacology and kinetics of the receptor response. Expand
Determination of the minimal functional ligand-binding domain of the GABAB1b receptor.
TLDR
T truncated GABA(B1) receptors are designed to identify the minimal functional domain which still binds a competitive radioligand and leads to a functional, GABA-responding receptor when co-expressed with GABA(b2) and the absence of oligosaccharides does not impair receptor function, suggesting that the unglycosylated ECD of GABA(Bs) can be used for further functional or structural investigations. Expand
GABAB Receptor Complex as a Potential Target for Tumor Therapy
  • Xinnong Jiang, L. Su, +4 authors Jianfeng Liu
  • Biology, Medicine
  • The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
  • 2012
TLDR
Their structural complexity makes it possible to disrupt the functions of GABAB receptors in various ways, raising GABAB receptor diversity as a potential therapeutic target in some human cancers. Expand
Mechanisms of GABA A and GABA B Receptor Gene Regulation and Cell Surface Expression
The γ-aminobutyric acid (GABA) neurotransmitter acting through ionotropic and metabotropic receptor classes exerts the major inhibitory control in the central nervous system. Therapeutic agentsExpand
The expression of GABAB1 and GABAB2 receptor subunits in the cNS differs from that in peripheral tissues
TLDR
These areas are of interest as they may well contain novel GABA(B) receptor subunit isoforms, expression of which would enable the GABA(B1) subunit to reach the cell surface and form functional GABA( B) receptors. Expand
Investigations into GABAB receptor surface stability and molecular interactions.
TLDR
The results presented in this thesis suggest GABAB receptors are highly stable at the neuronal surface and the activation of PKA and AMPK may be mechanisms by which neurones are able to regulate plasma membraneGABAB receptors. Expand
The C-Terminal Domains of the GABAB Receptor Subunits Mediate Intracellular Trafficking But Are Not Required for Receptor Signaling
TLDR
Although GABAB1 is capable of producing GABA-binding sites, GABAB2 is of central importance in the functional coupling of heteromeric GABAB receptors to G-proteins and the subsequent activation of effector systems. Expand
The GABAB Receptor
γ-Aminobutyric acid (GABA) is the prevalent inhibitory neurotransmitter in the brain. It exerts it action through ligand-gated Cl- channel (GABAA and GABAC receptors) and G protein coupled receptorsExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 27 REFERENCES
Intracellular Retention of Recombinant GABABReceptors*
TLDR
It is reported that recombinant GABAB receptors fail to reach the cell surface when expressed in heterologous systems and are retained in the endoplasmic reticulum when introduced into COS cells and proved that they fail to activate in superior cervical ganglion neurons. Expand
Expression cloning of GABAB receptors uncovers similarity to metabotropic glutamate receptors
TLDR
The cloning of GABAB receptors is reported and photoaffinity labelling experiments suggest that the cloned receptors correspond to two highly conserved GABAB receptor forms present in the vertebrate nervous system. Expand
Structural and functional aspects of G protein-coupled receptor oligomerization.
TLDR
Evidence is reviewed that receptor oligomerization and in particular dimerization may play an important role in the molecular events leading to GPCR activation, and biochemical and functional evidence supporting this notion is reviewed. Expand
Structural and functional aspects of G protein-coupled receptor oligomerization.
TLDR
Evidence is reviewed that receptor oligomerization and in particular dimerization may play an important role in the molecular events leading to GPCR activation, and biochemical and functional evidence supporting this notion is reviewed. Expand
A Peptide Derived from a β2-Adrenergic Receptor Transmembrane Domain Inhibits Both Receptor Dimerization and Activation*
TLDR
It is demonstrated that β2-adrenergic receptors do form SDS-resistant homodimers and that transmembrane domain VI of the receptor may represent part of an interface for receptor dimerization, which suggests that interconversion between monomeric and dimeric forms may be important for biological activity. Expand
Metabotropic Glutamate Receptor 5 Is a Disulfide-linked Dimer*
TLDR
mGluR5, as well as other mGluRs, behave as species approximately twice as large as expected from their sequence, but reducing conditions cause a decrease to the predicted molecular mass, due to specific, disulfide-dependent dimerization of the receptor. Expand
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
TLDR
The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses. Expand
Homer: a protein that selectively binds metabotropic glutamate receptors
TLDR
A novel dendritic protein, Homer, is reported that contains a single, PDZ-like domain and binds specifically to the carboxy terminus of phosphoinositide-linked metabotropic glutamate receptors, suggesting that Homer mediates a novel cellular mechanism that regulates glutamate signalling. Expand
μ and δ Opioid Receptors Are Differentially Desensitized by the Coexpression of β-Adrenergic Receptor Kinase 2 and β-Arrestin 2 in Xenopus Oocytes*
TLDR
These studies establish that opioid receptors can be regulated by β-ARK2 and β-arr2 and that a portion of the COOH terminus of DOR enhances sensitivity to this modulation. Expand
Dimerization of the delta opioid receptor: implication for a role in receptor internalization.
TLDR
The results suggest that the interconversion between the dimeric and monomeric forms plays a role in opioid receptor internalization. Expand
...
1
2
3
...