GRIN1
GRIN1 (GluN1, NR1, NMDAR1) encodes the glycine-binding subunit that is an essential component of N-methyl-D-aspartate (NMDA) receptors. These ligand-gated cation channels contribute to synaptic plasticity, learning and memory. Browse Assay Genie's current range of GRIN1 research reagents below, or read on for the biology behind the target.
GRIN1 is a component of N-methyl-D-aspartate receptors (NMDARs), which function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+). Channel activation requires three conditions: binding of the neurotransmitter L-glutamate to the GluN2 subunit, binding of glycine or D-serine to the GluN1 subunit, and membrane depolarisation to relieve inhibition by Mg(2+). Once open, NMDARs mediate potassium efflux together with the influx of calcium and sodium.
NMDARs participate in synaptic plasticity for learning and memory formation by contributing to long-term potentiation (LTP). The NCBI Gene summary describes the GRIN1 gene product as a critical subunit of these receptors, which belong to the glutamate receptor channel superfamily and form heteromeric complexes of multiple subunits. Each GluN2 or GluN3 subunit that partners with GluN1 confers distinct channel properties, including activation, deactivation and desensitisation kinetics, pH sensitivity, Ca2+ permeability and binding to allosteric modulators. Partner subunits include GRIN2A, GRIN2B and GRIN2D.
The GluN1 protein is found at the cell membrane, including the postsynaptic cell membrane and postsynaptic density membrane. It belongs to the glutamate-gated ion channel family (TC 1.A.10.1), NR1/GRIN1 subfamily, and the HGNC places it in the group of glutamate ionotropic receptor NMDA type subunits. The gene was previously named N-methyl-D-aspartate receptor subunit NR1. Alternatively spliced transcript variants have been described, and cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits.
GluN1-containing NMDARs contribute to long-term potentiation, making GRIN1 central to studies of synaptic plasticity.
NMDAR signalling is believed to underlie learning and memory, so GRIN1 is a key subunit for investigating these processes.
Glycine or D-serine binding to GluN1 and allosteric modulation by partner subunits make GRIN1 relevant to channel gating studies.
GluN1 assembles with GluN2 or GluN3 subunits that tune channel kinetics, so GRIN1 is a reference point for NMDAR composition.
GRIN1 encodes GluN1, a subunit of NMDA receptors, which are heterotetrameric ligand-gated cation channels. GluN1 binds glycine or D-serine, while glutamate binds GluN2. With depolarisation to remove Mg(2+) block, the channel passes calcium and sodium, supporting long-term potentiation, synaptic plasticity, learning and memory.
GRIN1 is also known as GluN1, NR1 and NMDAR1. Its HGNC name is glutamate ionotropic receptor NMDA type subunit 1, and earlier names include N-methyl-D-aspartate receptor subunit NR1. Alternatively spliced transcript variants have been described, and the UniProt protein name is Glutamate receptor ionotropic, NMDA 1.
Yes. Orthologues of the human gene, named Grin1, exist in both mouse and rat. Researchers working in rodent models of synaptic function can therefore study the equivalent subunit; check the datasheet of any product for its validated reactivity.
Other NMDA receptor subunits and related glutamate receptor targets for synaptic signalling research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q05586; product specifications from Assay Genie datasheets.