Aliases for GRIA1 Gene
External Ids for GRIA1 Gene
Previous Symbols for GRIA1 Gene
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. This gene belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for GRIA1 Gene
GRIA1 (Glutamate Receptor, Ionotropic, AMPA 1) is a Protein Coding gene. Diseases associated with GRIA1 include limbic encephalitis. Among its related pathways are CREB Pathway and CREB Pathway. GO annotations related to this gene include PDZ domain binding and glutamate receptor activity. An important paralog of this gene is GRID2.
UniProtKB/Swiss-Prot for GRIA1 Gene
Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.
AMPA receptors are members of the ionotropic class of glutamate receptors, which also includes NMDA and kainate receptors. AMPA receptors mediate fast excitatory synaptic transmission in the CNS and play a key role in hippocampal synaptic long-term potentiation (LTP) and depression (LTD). AMPA receptors consist of GluR1-4 subunits which assemble as homomers or heteromers to form functional AMPA receptors. The subunit composition determines the physiological properties of AMPA receptors: those containing the GluR2 subunit show low permeability to Ca2+ whereas those lacking this subunit show high Ca2+ permeability.