Biology:GRIA1

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Short description: Mammalian protein found in Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Glutamate receptor 1 is a protein that in humans is encoded by the GRIA1 gene.[1][2]

Function

Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. The GRIA1 belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Each of the members (GRIA1–4) include flip and flop isoforms generated by alternative RNA splicing. The receptor subunits encoded by each isoform vary in their signal transduction properties. The isoform presented here is the flop isoform. In situ hybridization experiments showed that human GRIA1 mRNA is present in granule and pyramidal cells in the hippocampal formation.[3]

GRIA1 (GluR1) is centrally involved in synaptic plasticity. Expression of the GluR1 gene is significantly reduced in the human frontal cortex with increasing age.[4]

Interactions

GRIA1 has been shown to interact with:

See also

  • AMPA receptor

References

  1. "Molecular cloning and chromosomal localization of one of the human glutamate receptor genes". Proc Natl Acad Sci U S A 88 (17): 7557–7561. October 1991. doi:10.1073/pnas.88.17.7557. PMID 1652753. Bibcode1991PNAS...88.7557P. 
  2. "Chromosomal localization of human glutamate receptor genes". J Neurosci 12 (7): 2555–2562. July 1992. doi:10.1523/JNEUROSCI.12-07-02555.1992. PMID 1319477. 
  3. "Entrez Gene: GRIA1 glutamate receptor, ionotropic, AMPA 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2890. 
  4. "Gene regulation and DNA damage in the ageing human brain". Nature 429 (6994): 883–891. June 2004. doi:10.1038/nature02661. PMID 15190254. Bibcode2004Natur.429..883L. 
  5. "CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction". J. Biol. Chem. 278 (45): 44745–44752. November 2003. doi:10.1074/jbc.M303576200. PMID 12933808. 
  6. "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit". J. Biol. Chem. 273 (31): 19518–19524. July 1998. doi:10.1074/jbc.273.31.19518. PMID 9677374. 
  7. "Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway". J. Neurosci. 21 (19): 7506–7516. October 2001. doi:10.1523/JNEUROSCI.21-19-07506.2001. PMID 11567040. 
  8. "Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association". J. Neurosci. 20 (21): 7932–7940. November 2000. doi:10.1523/JNEUROSCI.20-21-07932.2000. PMID 11050113. 
  9. "Heteromer formation of delta2 glutamate receptors with AMPA or kainate receptors". Brain Res. Mol. Brain Res. 110 (1): 27–37. January 2003. doi:10.1016/s0169-328x(02)00561-2. PMID 12573530. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.