Introduction of GRIN1
N-Methyl-D-aspartate (NMDA) receptors (NMDARs) are ionotropic glutamate receptors that play a critical role in excitatory neurotransmission in the central nervous system (CNS). Functional NMDARs are tetramers composed of different subunits: GRIN1, GRIN2A-D, GRIN3A-B. Structurally, GRINs share a common membrane topology: three transmembrane segments (M1, M3, M4) and a re-entrant pore loop (M2). The gene of GRIN1, GRIN1, is alternatively spliced, producing eight distinct isoforms differing in the C-terminus. This could modulate NMDAR trafficking. GRIN1 shows a region- and age-dependent expression pattern. It is uniformly expressed in the CNS before birth but displays isoform-specific differences in expression. Moreover, the subcellular expression of GRIN1 exists either in the plasma membrane or retention in the ER.
|Basic Information of GRIN1|
|Protein Name||Glutamate receptor ionotropic, NMDA 1|
|Gene Name||GRIN1, NMDAR1|
|Organism||Homo sapiens (Human)|
Functions of GRIN1 Membrane Protein
GRIN1 is the product of a single gene and is an obligatory subunit of all endogenous NMDA receptors. Studies have shown that the genetic elimination of GRIN1 is lethal in neonatal stages and that the NMDARs of GRIN1-deficient mice are dysfunctional because the GRIN2 is retained in the ER. Moreover, GRIN1 influences some properties of NMDARs such as their inhibition by protons or zinc, as well as their potentiation by polyamines. Additionally, the C-terminus of the GRIN1 subunit contains several motifs that regulate receptor trafficking and binding to many proteins. Mislocalization and abnormal trafficking of NMDARs are implicated in brain disorders and pathological conditions such as Parkinson’s disease, Huntington’s disease, ischemia, and stroke.
Application of GRIN1 Membrane Protein in Literature
This study examined the effects of RNAi of GluN1 protein on the subthreshold oscillations of neurons in the inferior olive, a pacemaking nucleus necessary for motor and cognitive timing.
This study investigated whether magnesium restriction (MgR) induced changes in brain NMDA receptor subunit composition. The results showed that MgR was associated with reduced amygdala-hypothalamic protein levels of GluN1-containing NMDA complexes.
Using the atomic force microscopy (AFM) imaging, the interaction between the σ-1 receptor (Sig1R) and the NMDAR was investigated. The results showed that the Sig1R bound to the GluN1/GluN2A NMDAR specifically via the GluN1 subunit.
This study tested the interactions among alcohol-sensitive positions at the M domain intersubunit interfaced in GluN1/GluN2B NMDA receptors, using tsA201 cells expressing tryptophan substitution mutants at ethanol-sensitive positions in the GluN1 and GluN2B NMDA receptor subunits. The manner in which the GluN2A and GluN2B subunits interacted with the GluN1 subunit to regulate ethanol sensitivity and receptor kinetics was different.
This study investigated the effect of remifentanil (μ-opioid receptor agonist), along with ketamine (NMDAR antagonist) and naloxone (μ-opioid receptor antagonist), on GluN1 mRNA levels and the amount of phosphorylated GluN1 in primary cultures of embryonic rat dorsal horn neurons (DHNs).
GRIN1 Preparation Options
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