GRIA 2

Glutamate receptor, ionotropic, AMPA 2
Properties of human protein
Mass / length primary structure	859 amino acids
Secondary to quaternary structure	multipass membrane protein; Homo- / heterotetramer
Isoforms	Flip, flop, long
Identifier
Gene names	GRIA2 ; GLUR2
External IDs	OMIM : 138247 ; UniProt : P42262 ; MGI : 95809 ;
Transporter classification
TCDB	1.A.10
designation	Glutamate-gated ion channel
Occurrence
Homology family	CG3822 PA
Parent taxon	Bilateria
	Orthologue

The ionotropic glutamate receptor AMPA 2 (Syn .: GRIA2) belongs to the group of AMPA receptors . It's a human protein . Glutamate receptors are the predominant form of excitatory neurotransmitter receptors in the mammalian brain . They are activated by a variety of neurophysiological processes. This membrane protein belongs to the family of glutamate receptors, which are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA). It is a ligand-activated cation channel. These channels are composed of the four sub-units GRIA1-4. In the case of the gene of the subunit GRIA2, an RNA editing (CAG-> CGG; Q-> R) is described within the section which codes for the second transmembrane domain. This presumably makes the canal Ca (2+) impermeable. Human and animal studies suggest that pre-mRNA editing is essential for normal brain function, and that errors in RNA editing of the GRIA2 gene play a role in causing ALS . An alternative splicing has been described for this gene , which results in the formation of so-called flip-flop isoforms, which differ in their signal transmission properties.

Recommended literature

MM Soundarapandian, WH Tu, PL Peng et al: AMPA receptor subunit GluR2 gates injurious signals in ischemic stroke. In: Mol. Neurobiol. vol. 32,2, 2007, pp. 145-155. PMID 16215279
W. Sun, AV Ferrer-Montiel, AF Schinder et al: Molecular cloning, chromosomal mapping, and functional expression of human brain glutamate receptors. In: Proc. Natl. Acad. Sci. USA vol. 89,4, 1992, pp. 1443-1447. PMID 1311100
JO McNamara, JH Eubanks, JD McPherson and others: Chromosomal localization of human glutamate receptor genes. In: J. Neurosci. vol. 12, 7, 1992, pp. 2555-2562. PMID 1319477
B. Sommer, K. Keinänen, TA Verdoorn et al .: Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS. In: Science. vol. 249, 4976, 1990, pp. 1580-1585. PMID 1699275
B. Sommer, M. Köhler, R. Sprengel, PH Seeburg: RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. In: Cell. vol. 67, 1, 1991, pp. 11-19. PMID 1717158
W. Paschen, JC Hedreen, CA Ross: RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue. In: J. Neurochem. vol. 63,5, 1994, pp. 1596-1602. PMID 7523595
M. Köhler, HC Kornau, PH Seeburg: The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B. In: J. Biol. Chem. Vol. 269,26, 1994, pp. 17367-17370. PMID 7545935
SL Eastwood, PW Burnet, J. Beckwith et al: AMPA glutamate receptors and their flip and flop mRNAs in human hippocampus. In: Neuroreport. vol. 5,11, 1994, pp. 1325-1328. PMID 7919190
W. Sun, AV Ferrer-Montiel, M. Montal: Primary structure and functional expression of the AMPA / kainate receptor subunit 2 from human brain. In: Neuroreport. vol. 5.4, 1994, pp. 441-444. PMID 8003671
M. Higuchi, FN Single, M. Köhler et al: RNA editing of AMPA receptor subunit GluR-B: a base-paired intron-exon structure determines position and efficiency. In: Cell. vol. 75, 7, 1994, pp. 1361-1370. PMID 8269514
DP McLaughlin, ME Cheetham, RW Kerwin: Expression of alternatively-spliced glutamate receptors in human hippocampus. In: Eur. J. Pharmacol. vol. 244, 1, 1993, pp. 89-92. PMID 8420792
S. Srivastava, P. Osten, FS Vilim et al: Novel anchorage of GluR2 / 3 to the postsynaptic density by the AMPA receptor-binding protein ABP. In: Neuron. vol. 21,3, 1998, pp. 581-591. PMID 9768844
S. Matsuda, S. Mikawa, H. Hirai: Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein. In: J. Neurochem. vol. 73,4, 1999, pp. 1765-1768. PMID 10501226
H. Hirai, S. Matsuda: Interaction of the C-terminal domain of delta glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells. In: Neurosci. Res. Vol. 34,4, 2000, pp. 281-287. PMID 10576550
PJ Aruscavage, BL Bass: A phylogenetic analysis reveals an unusual sequence conservation within introns involved in RNA editing. In: RNA. vol. 6.2, 2000, pp. 257-269. PMID 10688364
P. Osten, L. Khatri, JL Perez et al .: Mutagenesis reveals a role for ABP / GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. In: Neuron. vol. 27,2, 2000, pp. 313-325. PMID 10985351
HJ Chung, J. Xia, RH Scannevin et al: Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. In: J. Neurosci. vol. 20, 19, 2001, pp. 7258-7267. PMID 11007883
N. Armstrong, E. Gouaux: Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. In: Neuron. vol. 28.1, 2000, pp. 165-181. PMID 11086992
K. Krampfl, F. Schlesinger, A. Zörner et al: Control of kinetic properties of GluR2 flop AMPA-type channels: impact of R / G nuclear editing. In: Eur. J. Neurosci. vol. 15,1, 2002, pp. 51-62. PMID 11860506
H. Hirbec, O. Perestenko, A. Nishimune et al: The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs. In: J. Biol. Chem. Vol. 277, 18, 2002, pp. 15221-15224. PMID 11891216

Individual evidence

↑ ^a ^b Entrez Gene: GRIA2 glutamate receptor, ionotropic, AMPA 2. Accessed December 31, 2010 .

[entrez-1] Entrez Gene: GRIA2 glutamate receptor, ionotropic, AMPA 2. Accessed December 31, 2010 .