Interaction between GABAA receptor subunit intracellular loops: Implications for higher order complex formation

Journal of Neurochemistry

Volumn 83, Issue 5, 2002, Pages 1164-1171

  Nymann Andersen, Jesper ^a   Wang, Hongbing ^b   Sawyer, Gregory W ^c   Olsen, Richard W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

2 subunit; GABAA receptor; GABAA receptor targeting; GABAA receptor associated protein; Intracellular loop

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; 4 AMINOBUTYRIC ACID A RECEPTOR ASSOCIATED PROTEIN; AMINO ACID; CHLORIDE CHANNEL; GLUTATHIONE TRANSFERASE; LIGAND; PEPTIDE; PROTEIN; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG; HYBRID PROTEIN; PEPTIDE FRAGMENT; PROTEIN SUBUNIT;

AMINO ACID ANALYSIS; ARTICLE; ASSAY; CENTRAL NERVOUS SYSTEM; CHANNEL GATING; COMPLEX FORMATION; DISSOCIATION CONSTANT; HYBRID; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; YEAST; AMINO ACID SEQUENCE; ANIMAL; BIOLOGICAL MODEL; CAPPING PHENOMENON; CATTLE; CHEMISTRY; GENETICS; MACROMOLECULE; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; TWO HYBRID SYSTEM;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; GLUTATHIONE TRANSFERASE; MACROMOLECULAR SUBSTANCES; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECEPTOR AGGREGATION; RECEPTORS, GABA-A; RECOMBINANT FUSION PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0036884782     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2002.01222.x     Document Type: Article

References (48)

1. Banerjee A., Srilatha N. S. and Murthy G. S. (2002) Real-time kinetic analysis of hCG-monoclonal antibody interaction using radiolabeled hCG probe: Presence of two forms of Ag-mAb complex as revealed by solid phase dissociation studies. Biochim. Biophys. Acta 1569, 21-30.
2. A receptors suggest differential targeting of receptor subtypes. J. Neurosci. 19, 2960-2973.
3. A receptor subunits in primary cultures of rat cerebellar granule cells. Neuroscience 67, 583-593.
4. A receptor clustering and modulates the channel kinetics. Proc. Natl. Acad. Sci. USA 97, 11557-11562.
5. Craig A. M., Blackstone C. D., Huganir R. L. and Banker G. (1994) Selective clustering of glutamate and γ-aminobutyric acid receptors opposite terminals releasing the corresponding neurotransmitters. Proc. Natl. Acad. Sci. USA 91, 12373-12377.
6. A receptors by rapsyn. Neurochem. Int. 34, 453-463.
7. A channel conductance increased by diazepam. Nature 388, 71-75.
8. Ehlers M. D., Mammen A. L., Lau L. F. and Huganir R. L. (1996) Synaptic targeting of glutamate receptors. Curr. Opin. Cell Biol. 8, 484-489.
9. A/benzodiazepine receptor complex. Adv. Exp. Med. Biol. 287, 375-380.
10. A receptor subtypes requires the γ2 subunit and gephyrin. Nat. Neurosci. 1, 563-571.
11. A/benzodiazepine receptor. J. Cell Biol. 110, 2043-2048.
12. Feng G., Tintrup H., Kirsch J., Nichol M. C., Kuhse J., Betz H. and Sanes J. R. (1998) Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity. Science 282, 1321-1324.
13. Fields S. and Song O. K. (1989) A novel genetic system to detect protein-protein interactions. Nature (London) 340, 245-246
14. A-receptor heterogeneity in the adult rat brain: Differential regional and cellular distribution of seven major subunits. J. Comp. Neurol. 359, 154-194.
15. Froehner S. C. (1993) Regulation of ion channel distribution at synapses. Annu. Rev. Neurosci. 16, 347-368.
16. Gietz D., St Jean A., Woods R. A. and Schiestl R. H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucl. Acids Res. 20, 1425-1431.
17. A sub-units specify their selective interaction in vitro. J. Neurochem. 70, 40-46.
18. Haring P., Stahli C., Schoch P., Takacs B., Staehelin T. and Mohler H. (1985) Monoclonal antibodies reveal structural homogeneity of γ-aminobutyric acid/benzodiazepine receptors in different brain areas. Proc. Natl. Acad. Sci. USA 82, 4837-4841.
19. Hill J. A. Jr (1992) Nicotinic receptor-associated 43K protein and progressive stabilization of the postsynaptic membrane. Mol. Neurobiol. 6, 1-17.
20. Kirsch J., Langosch D., Prior P., Littauer U. Z., Schmitt B. and Betz H. (1991) The 93-kDa glycine receptor-associated protein binds to tubulin. J. Biol. Chem. 266, 22242-22245.
21. Kirsch J., Wolters I., Triller A. and Betz H. (1993) Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons. Nature 366, 745-748.
22. Kirsch J., Kuhse J. and Betz H. (1995) Targeting of glycine receptor subunits to gephyrin-rich domains in transfected human embryonic kidney cells. Mol. Cell. Neurosci. 6, 450-461.
23. A receptors. Mol. Cell. Neurosci. 18, 13-25.
24. A receptor assembly. Identification and structure of γ2 sequences forming the intersubunit contacts with α1 and β3 subunits. J. Biol. Chem. 275, 8921-8928.
25. A receptor clustering in gephyrin-deficient mice. J. Neurosci. 19, 9289-9297.
26. Kneussel M., Haverkamp S., Fuhrmann J. C., Wang H., Wässle H., Olsen R. W. and Betz H. (2000) The γ-aminobutyric acid type A receptor (GABAR)-associated protein GABARAP interacts with gephyrin but is not involved in receptor anchoring at the synapse. Proc. Natl. Acad. Sci. USA 97, 8594-8599.
27. A receptors on cerebellar granule cells as determined by a quantitative immunogold method. J. Neurosci. 15, 2948-2960.
28. A receptors. J. Neurochem. 80, 815-823.
29. A receptor-associated protein (GABARAP) mediating dimer formation. Neuropharmacology 43, 476-481.
30. A receptor complex: Structure and function, in Glutamate and GABA Receptors and Transporters. Structure, Function and Pharmacology, 1st Edition (Egebjerg J., Schousboe A. and Krogsgaard-Larsen P., eds), pp. 202-235. Taylor and Francis, London.
31. Phillips W. D., Kopta C., Blount P., Gardner P. D., Steinbach J. H. and Merlie J. P. (1991) ACh receptor-rich membrane domains organized in fibroblasts by recombinant 43-kildalton protein. Science 251, 568-570.
32. 3H]Ro15-4513. J. Biol. Chem. in press.
33. Sheng M. and Wyszynski M. (1997) Ion channel targeting in neurons. Bioessays 19, 847-853.
34. 3H]Ro15-4513: A biochemical and autoradiographic study. J. Neurochem. 48, 46-52.
35. Sigel E., Mamalaki C. and Barnard E. A. (1982) Isolation of a GABA receptor from bovine brain using a benzodiazepine affinity column. FEBS Lett. 147, 45-48.
36. Slepak V. Z. (2000) Application of surface plasmon resonance for analysis of protein-protein interactions in the G protein-mediated signal transduction pathway. J. Mol. Recognit. 13, 20-26.
37. A receptor is concentrated in synaptic junctions containing the α1 and β2/3 subunits in hippocampus, cerebellum and globus pallidus. Neuropharmacology 35, 1425-1444.
38. A receptor subunits in the rat hippocampus I: Immunocytochemical distribution of 13 subunits. Neuroscience 80, 987-1000.
39. A receptor assembly. J. Biol. Chem. 274, 26633-26638.
40. Stauber G. B., Ransom R. W., Dilber A. I. and Olsen R. W. (1987) The γ-aminobutyric acid/benzodiazepine-receptor protein from rat brain: Large-scale purification and preparation of antibodies. Eur. J. Biochem. 167, 125-134.
41. A receptor β subunits that mediate both homomeric and heteromeric receptor expression. J. Neurosci. 19, 6360-6371.
42. A receptor subtype that is insensitive to diazepam. J. Pharmacol. Exp. Ther. 257, 1236-1242.
43. Vannier C. and Triller A. (1997) Biology of the postsynaptic glycine receptor. Int. Rev. Cytol. 176, 201-244.
44. Velazquez J. L., Thompson C. L., Barnes E. M. Jr and Angelides K. J. (1989) Distribution and lateral mobility of GABA/benzodiazepine receptors on nerve cells. J. Neurosci. 9, 2163-2169.
45. A receptor interaction. J. Neurochem. 75, 644-655.
46. A receptors and the cytoskeleton. Nature 397, 69-72.
47. A receptors by rapsyn/43kD protein in vitro. Mol. Cell. Neurosci. 8, 430-438.
48. Zervos A. S., Gyuris J. and Brent R. (1993) Mxil, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72, 223-232.