GRIA1
GRIA1 (glutamate ionotropic receptor AMPA type subunit 1, also known as GluA1, GLURA and GLUR1) is a subunit of the AMPA-type ionotropic glutamate receptor. It forms a ligand-gated cation channel that converts the chemical signal of L-glutamate into an electrical impulse at excitatory synapses. Browse Assay Genie's current range of GRIA1 research reagents below, or read on for the biology behind the target.
GRIA1 is an ionotropic glutamate receptor that works as a ligand-gated cation channel. It is gated by L-glutamate and by agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid and kainic acid. L-glutamate is an excitatory neurotransmitter at many synapses in the central nervous system. When it binds, the receptor changes conformation and the channel opens. Monovalent and divalent cations, such as sodium and calcium, can then enter, and the chemical signal becomes an electrical one. The receptor then desensitises rapidly and enters a transient inactive state with agonist still bound.
Channel behaviour depends on the subunits and partner proteins in the complex. In the presence of CACNG2, CACNG4, CACNG7 or CACNG8, GRIA1 shows resensitisation, seen as a delayed build-up of current during continued glutamate application. CNIH2 blocks this resensitisation through interaction with CACNG8 in CACNG8-containing AMPA receptor complexes. Calcium permeability also depends on subunit composition, and heteromeric channels that contain edited GRIA2 subunits are calcium-impermeable. The channel is also permeable to strontium, magnesium, potassium and lithium ions.
Glutamate receptors are the main excitatory neurotransmitter receptors in the mammalian brain. They act as heteromeric complexes of several subunits, each with transmembrane regions, arranged to form a ligand-gated ion channel. The GRIA1 gene belongs to the AMPA receptor family, and the protein belongs to the glutamate-gated ion channel family, GRIA1 subfamily. The HGNC previously named it glutamate receptor, ionotropic, AMPA 1. UniProt places the protein in the cell membrane, endoplasmic reticulum membrane, postsynaptic density membrane, dendritic spines, and early and recycling endosome membranes. Alternatively spliced transcript variants encode different isoforms. Researchers studying the GRIA1 gene or GRIA1 protein often do so in the context of synaptic transmission.
GRIA1 helps convert glutamate binding into electrical signals at excitatory synapses in the central nervous system.
Subunit composition, including partnership with GRIA2, determines how AMPA receptor channels behave and whether they pass calcium.
CACNG subunits and CNIH2 modulate resensitisation in AMPA receptor complexes that contain GRIA1.
GRIA1 is found in dendritic spines, the postsynaptic density, and early and recycling endosome membranes.
GRIA1 is a subunit of AMPA-type ionotropic glutamate receptors. It forms a ligand-gated cation channel that opens when L-glutamate binds, letting sodium and calcium enter and generating an electrical impulse. The receptor then desensitises rapidly and enters a transient inactive state.
GRIA1 is also called GluA1, GLURA and GLUR1. Its UniProt name is glutamate receptor 1, and its previous HGNC name was glutamate receptor, ionotropic, AMPA 1. Alternatively spliced transcript variants have been reported to encode different isoforms.
Yes. Mouse and rat both have a Gria1 ortholog. Related AMPA receptor subunits GRIA2, GRIA3 and GRIA4 are also present in the family. Check the datasheet of any product for its validated reactivity.
Other AMPA receptor subunits that form heteromeric glutamate-gated channels with GRIA1.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P42261; product specifications from Assay Genie datasheets.