GRIA3 Membrane Protein Introduction

Introduction of GRIA3

Glutamate receptor 3 (GRIA3), also known as AMPA-selective glutamate receptor 3, is a protein that in humans is encoded by the GRIA3 (or GLUR3) gene. Glutamate receptor 3 is a member of the glutamate receptor family, which are the major excitatory neurotransmitter receptors in the mammalian brain. These receptor proteins are heteromeric protein complexes and have multiple subunits. Each of them has transmembrane regions. All are arranged to form a ligand-gated ion channel. Glutamate receptors can be activated in different normal neurophysiologic processes. 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. Alternative splicing, resulting in transcript variants encoding different isoforms, has been noted for this gene, which includes the generation of flip and flop isoforms that vary in their signal transduction properties.

Basic Information of GRIA3
Protein Name Glutamate receptor 3
Gene Name GRIA3
Aliases GluR-3, AMPA-selective glutamate receptor 3, GluR-C, GluR-K3, Glutamate receptor ionotropic, AMPA 3, GluA3, GLUR3, GLuA3
Organism Homo sapiens (Human)
UniProt ID P42263
Transmembrane Times 3
Length (aa) 894

Function of GRIA3 Membrane Protein

Glutamate, a major excitatory neurotransmitter, is known to play a key role in the regulation of sleep. In rats, wakefulness and sleep are characterized by changes in extracellular glutamate levels, as well as changes in the level and phosphorylation state of GluA1-containing alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA)-type ionotropic glutamate receptors (AMPARs) (encoded by Gria1), important mediators of synaptic transmission and plasticity. A pathogenic mutation in the GRIA3 gene encoding the GluA3 subunit of AMPARs is found in a family with an apparently novel disorder: severe sleep and circadian rhythm disruption, with a greatly lengthened sleep-wake cycle that progressively lengthened over the decade following puberty, combined with profound intellectual disability (ID) and developmental delay. Several diseases are associated with GRIA3 including mental retardation, x-linked, syndromic, wu type, and Rasmussen encephalitis.

Physical map of GRIA3.Fig.1 Physical map of GRIA3.

Application of GRIA3 Membrane Protein in Literature

  1. Renner M.C., et al. Synaptic plasticity through activation of GluA3-containing AMPA-receptors. Elife. 2017. PubMed ID: 28762944

    This article uncovers a new type of plasticity at CA1 hippocampal synapses. It is expressed by the activation of GluA3-containing AMPARs.

  2. Davies B., et al. A point mutation in the ion conduction pore of AMPA receptor GRIA3 causes dramatically perturbed sleep patterns as well as intellectual disability. Hum Mol Genet. 2017, 26(20): 3869-3882. PubMed ID: 29016847

    Authors in this group demonstrate that GluA3 channel activity plays a role in the regulation of sleep behavior in both mice and humans.

  3. Wei C.H., et al. MicroRNA-330-3p promotes cell invasion and metastasis in non-small cell lung cancer through GRIA3 by activating MAPK/ERK signaling pathway. J Hematol Oncol. 2017, 10(1): 125. PubMed ID: 28629431

    The article explores the underlying mechanism by which miR-330-3p promotes cell migration and invasion of NSCLC. The results suggest that miR-330-3p promotes the progression of NSCLC, which can be used as a potential target for the further study of NSCLC brain metastasis.

  4. Gutierrez-Castellanos N., et al. Motor Learning Requires Purkinje Cell Synaptic Potentiation through Activation of AMPA-Receptor Subunit GluA3. Neuron. 2017, 93(2): 409-424. PubMed ID: 28103481

    The article reveals that vestibulo-cerebellar motor learning is the first form of memory acquisition. Increased single-channel conductance is shown to be dependent on GluA3-dependent synaptic potentiation.

  5. García-Hernández S., et al. Impaired auditory processing and altered structure of the endbulb of Held synapse in mice lacking the GluA3 subunit of AMPA receptors. Hear Res. 2017, 344: 284-294. PubMed ID: 28011083

    This article reports that GluA3 is required for normal auditory signaling, normal ultrastructure of AN-BC synapses in the cochlear nucleus and normal experience-dependent changes in auditory processing after transient sound reduction.

GRIA3 Preparation Options

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As a leading service provider, Creative Biolabs is proud to present our professional service in membrane protein preparation and help you with the research of membrane proteins. Please do not hesitate to inquire us for more details.

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