GRIA4

GRIA4
Glutamate receptor, ionotrophic, AMPA 4

Größe 882 Aminosäuren
Struktur Homo-/Heterotetramer, multipass Membranprotein
Bezeichner
Gen-Name GRIA4
Externe IDs OMIM138246 UniProtP48058   MGI95811
Transporter-Klassifikation
TCDB 1.A.10
Bezeichnung glutamatgesteuerter Ionenkanal
Orthologe
Mensch Maus
Entrez 2893 14802
Ensembl ENSG00000152578 ENSMUSG00000025892
UniProt P48058 Q8BXG8
Refseq (mRNA) NM_000829 NM_019691
Refseq (Protein) NP_000820 NP_062665
Genlocus Chr chr11: 104.99 - 105.36 Mb Chr chr9: 4.42 - 4.8 Mb
PubMed Suche [1] [2]

Der ionotrope Glutamate Rezeptor, AMPA 4, auch bekannt als GRIA4 oder GluR4, ist ein menschliches Protein.[1]

Dieses Membranprotein ist ein Mitglied der glutamatgesteuerten Ionenkanäle und vermittelt eine schnelle exzitatorische Signalübertragung an Synapsen. Der Kanaltyp kennt AMPA als Agonisten. Das Gen, das für dieses Protein kodiert gilt als eines der zahlreichen Schizophrenie-Kandidatengene. Für GRIA 4 sind durch alternatives Spleißen erzeugte mRNA-Varianten bekannt, die für verschiedene Isoformen der Proteinuntereinheiten codieren.[1]

Inhaltsverzeichnis

Siehe auch

AMPA-Rezeptor

Referenzen

  1. a b Entrez Gene: GRIA4 glutamate receptor, ionotrophic, AMPA 4.

Empfohlene Literatur

Further reading

  • McNamara JO, Eubanks JH, McPherson JD, et al.: Chromosomal localization of human glutamate receptor genes. in: J. Neurosci. vol. 12,7 pg. 2555–62 (1992) PMID 1319477
  • Hardy M, Younkin D, Tang CM, et al.: Expression of non-NMDA glutamate receptor channel genes by clonal human neurons. in: J. Neurochem. vol. 63,2 pg. 482–9 (1994) PMID 7518497
  • Roche KW, Raymond LA, Blackstone C, Huganir RL: Transmembrane topology of the glutamate receptor subunit GluR6. in: J. Biol. Chem. vol. 269,16 pg. 11679–82 (1994) PMID 8163463
  • Fletcher EJ, Nutt SL, Hoo KH, et al.: Cloning, expression and pharmacological characterization of a human glutamate receptor: hGluR4. in: Recept. Channels vol. 3,1 pg. 21–31 (1996) PMID 8589990
  • Bonaldo MF, Lennon G, Soares MB: Normalization and subtraction: two approaches to facilitate gene discovery. in: Genome Res. vol. 6,9 pg. 791–806 (1997) PMID 8889548
  • Ripellino JA, Neve RL, Howe JR: Expression and heteromeric interactions of non-N-methyl-D-aspartate glutamate receptor subunits in the developing and adult cerebellum. in: Neuroscience vol. 82,2 pg. 485–97 (1998) PMID 9466455
  • Carvalho AL, Kameyama K, Huganir RL: Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors. in: J. Neurosci. vol. 19,12 pg. 4748–54 (1999) PMID 10366608
  • Chen L, Chetkovich DM, Petralia RS, et al.: Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms. in: Nature vol. 408,6815 pg. 936–43 (2001) PMID 11140673
  • Hirbec H, Perestenko O, Nishimune A, 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 pg. 15221–4 (2002) PMID 11891216
  • Tomiyama M, Rodríguez-Puertas R, Cortés R, et al.: Flip and flop splice variants of AMPA receptor subunits in the spinal cord of amyotrophic lateral sclerosis. in: Synapse vol. 45,4 pg. 245–9 (2002) PMID 12125045
  • Pasternack A, Coleman SK, Jouppila A, et al.: Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain. in: J. Biol. Chem. vol. 277,51 pg. 49662–7 (2003) PMID 12393905
  • Correia SS, Duarte CB, Faro CJ, et al.: Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation. in: J. Biol. Chem. vol. 278,8 pg. 6307–13 (2003) PMID 12471040
  • Strausberg RL, Feingold EA, Grouse LH, et al.: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. in: Proc. Natl. Acad. Sci. U.S.A. vol. 99,26 pg. 16899–903 (2003) PMID 12477932
  • Makino C, Fujii Y, Kikuta R, et al.: Positive association of the AMPA receptor subunit GluR4 gene (GRIA4) haplotype with schizophrenia: linkage disequilibrium mapping using SNPs evenly distributed across the gene region. in: Am. J. Med. Genet. B Neuropsychiatr. Genet. vol. 116,1 pg. 17–22 (2003) PMID 12497607
  • Coleman SK, Cai C, Mottershead DG, et al.: Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein. in: J. Neurosci. vol. 23,3 pg. 798–806 (2003) PMID 12574408
  • Pasternack A, Coleman SK, Féthière J, et al.: Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain. in: J. Neurochem. vol. 84,5 pg. 1184–92 (2003) PMID 12603841
  • Kawahara Y, Ito K, Sun H, et al.: GluR4c, an alternative splicing isoform of GluR4, is abundantly expressed in the adult human brain. in: Brain Res. Mol. Brain Res. vol. 127,1-2 pg. 150–5 (2004) PMID 15306133
  • Li G, Sheng Z, Huang Z, Niu L: Kinetic mechanism of channel opening of the GluRDflip AMPA receptor. in: Biochemistry vol. 44,15 pg. 5835–41 (2005) PMID 15823042
  • Nuriya M, Oh S, Huganir RL: Phosphorylation-dependent interactions of alpha-Actinin-1/IQGAP1 with the AMPA receptor subunit GluR4. in: J. Neurochem. vol. 95,2 pg. 544–52 (2005) PMID 16190873
  • Kimura K, Wakamatsu A, Suzuki Y, et al.: Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. in: Genome Res. vol. 16,1 pg. 55–65 (2006) PMID 16344560

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