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GRIN1 Membrane Protein Introduction

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
Aliases NMD-R1
Organism Homo sapiens (Human)
UniProt ID Q05586
Transmembrane Times 3
Length (aa) 938
Sequence MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES

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.

GRIN1 Membrane Protein Introduction

Application of GRIN1 Membrane Protein in Literature

  1. Zhu Z., et al. RNA interference of GluN1 inhibits neuronal rhythmogenesis in the adult inferior olive. Journal of Molecular Neuroscience. 2015, 55(2): 416-429. PubMed ID: 24930901

    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.

  2. Ghafari M., et al. Dietary magnesium restriction reduces amygdala-hypothalamic GluN1 receptor complex levels in mice. Brain Structure & Function. 2015, 220(4): 2223-2223. PubMed ID: 24807818

    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.

  3. Balasuriya D., et al. The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor. Journal of Neuroscience the Official Journal of the Society for Neuroscience. 2013, 33(46): 18219-24. PubMed ID: 24227730

    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.

  4. Zhao Y., et al. Intersubunit interactions at putative sites of ethanol action in the M3 and M4 domains of the NMDA receptor GluN1 and GluN2B subunits. Br J Pharmacol. 2016, 173(12): 1950-1965. PubMed ID: 27010645

    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.

  5. Zhang C., et al. Phosphorylation of the GluN1 subunit in dorsal horn neurons by remifentanil: a mechanism for opioid-induced hyperalgesia. Genetics & Molecular Research Gmr. 2015, 14(1): 1846-54. PubMed ID: 25867330

    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

As a leader in providing both membrane protein products and solutions, Creative Biolabs now introduces our robust Magic™ Membrane Protein Production Platform to help promote your membrane protein studies. Our technical platform has extensive experience in reconstituting different types of membrane proteins, including GPCRs, ion channels, transporters, into functional and active formats for subsequent structural and functional studies. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-GRIN1 antibody development services.


Besides, as a custom-oriented service provider of antibody discovery and engineering, Creative Biolabs can also help with the discovery of anti-membrane protein antibodies. Please feel free to contact us for more information.

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