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GRIA2
Glutamate ionotropic receptor AMPA type subunit 2 (also known as glutamate receptor 2 or GluR-2) is a protein in humans that is encoded by the GRIA2 (also called GLUR2) gene. It functions as a subunit of AMPA receptors.
Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. This gene product belongs to a family of glutamate receptors that are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA), called AMPA receptors, and function as ligand-activated cation channels. These channels are assembled from a combination of 4 subunits, encoded by 4 genes (GRIA1-4). The subunit encoded by this gene (GRIA2) is subject to RNA editing which renders the receptor that it becomes part of impermeable to calcium ions (Ca2+). Human and animal studies suggest that the RNA editing is essential for normal brain function, and defective RNA editing of this gene may be relevant to the etiology of amyotrophic lateral sclerosis (ALS). 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.
GRIA2 has been shown to interact with SPTAN1, GRIP1 and PICK1.
The mRNAs of several ion channels and neurotransmitter receptor serve as substrates for ADARs. These include five subunits of glutamate-gated ion channels, specifically the ionotropic AMPA receptor subunits (GluR2, GluR3, GluR4) and kainate receptor subunits (GluR5, GluR6). Glutamate-gated ion channels are composed of four subunits per channel, with each subunit contributing to the pore loop structure. This pore loop is structurally related to that found in K+ channels, such as the human Kv1.1 channel. The pre-mRNA of the human Kv1.1 channel is also subject to A-to-I RNA editing. Glutamate receptors are responsible for mediating fast excitatory neurotransmission in the brain. The diversity of these receptors is generated through both alternative RNA splicing and RNA editing, which modify the coding sequences of individual subunits. GluR2, which is encoded by the pre-mRNA of the GRIA2 gene, is a well-studied example of a subunit that undergoes RNA editing.
The type of RNA editing that occurs in the pre-mRNA of GluR-2 is adenosine-to-inosine (A-to-I) editing. A-to-I RNA editing is catalyzed by a family of enzymes known as adenosine deaminases acting on RNA (ADARs), which specifically recognize adenosines within double-stranded regions of pre-mRNAs and convert them to inosine through deamination. Inosine is interpreted as guanosine by the cellular translational machinery.
There are three known members of the ADAR family: ADAR1, ADAR2, and ADAR3. Of these, only ADAR1 and ADAR2 are enzymatically active, while ADAR3 is believed to play a regulatory role, particularly in the brain. ADAR1 and ADAR2 are widely expressed across various tissues, whereas ADAR3 expression is restricted to the brain.
The double-stranded RNA (dsRNA) structures required for editing are typically formed through base-pairing between sequences near the editing site and complementary sequences, often located in a neighboring intron, although they can also be within exonic regions. The region that base-pairs with the editing site is referred to as the editing complementary sequence (ECS). ADARs bind to these dsRNA substrates via their double-stranded RNA-binding domains.
When an editing site is located within a coding region, A-to-I editing can result in a codon change, potentially altering the amino acid sequence of the resulting protein. This may lead to the production of a functionally distinct protein isoform. A-to-I editing also occurs in non-coding regions such as introns, untranslated regions (UTRs), and repetitive elements like LINEs and SINEs (especially Alu repeats). In these regions, editing may influence splicing, RNA stability, nuclear retention, and other aspects of RNA processing.
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GRIA2
Glutamate ionotropic receptor AMPA type subunit 2 (also known as glutamate receptor 2 or GluR-2) is a protein in humans that is encoded by the GRIA2 (also called GLUR2) gene. It functions as a subunit of AMPA receptors.
Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. This gene product belongs to a family of glutamate receptors that are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA), called AMPA receptors, and function as ligand-activated cation channels. These channels are assembled from a combination of 4 subunits, encoded by 4 genes (GRIA1-4). The subunit encoded by this gene (GRIA2) is subject to RNA editing which renders the receptor that it becomes part of impermeable to calcium ions (Ca2+). Human and animal studies suggest that the RNA editing is essential for normal brain function, and defective RNA editing of this gene may be relevant to the etiology of amyotrophic lateral sclerosis (ALS). 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.
GRIA2 has been shown to interact with SPTAN1, GRIP1 and PICK1.
The mRNAs of several ion channels and neurotransmitter receptor serve as substrates for ADARs. These include five subunits of glutamate-gated ion channels, specifically the ionotropic AMPA receptor subunits (GluR2, GluR3, GluR4) and kainate receptor subunits (GluR5, GluR6). Glutamate-gated ion channels are composed of four subunits per channel, with each subunit contributing to the pore loop structure. This pore loop is structurally related to that found in K+ channels, such as the human Kv1.1 channel. The pre-mRNA of the human Kv1.1 channel is also subject to A-to-I RNA editing. Glutamate receptors are responsible for mediating fast excitatory neurotransmission in the brain. The diversity of these receptors is generated through both alternative RNA splicing and RNA editing, which modify the coding sequences of individual subunits. GluR2, which is encoded by the pre-mRNA of the GRIA2 gene, is a well-studied example of a subunit that undergoes RNA editing.
The type of RNA editing that occurs in the pre-mRNA of GluR-2 is adenosine-to-inosine (A-to-I) editing. A-to-I RNA editing is catalyzed by a family of enzymes known as adenosine deaminases acting on RNA (ADARs), which specifically recognize adenosines within double-stranded regions of pre-mRNAs and convert them to inosine through deamination. Inosine is interpreted as guanosine by the cellular translational machinery.
There are three known members of the ADAR family: ADAR1, ADAR2, and ADAR3. Of these, only ADAR1 and ADAR2 are enzymatically active, while ADAR3 is believed to play a regulatory role, particularly in the brain. ADAR1 and ADAR2 are widely expressed across various tissues, whereas ADAR3 expression is restricted to the brain.
The double-stranded RNA (dsRNA) structures required for editing are typically formed through base-pairing between sequences near the editing site and complementary sequences, often located in a neighboring intron, although they can also be within exonic regions. The region that base-pairs with the editing site is referred to as the editing complementary sequence (ECS). ADARs bind to these dsRNA substrates via their double-stranded RNA-binding domains.
When an editing site is located within a coding region, A-to-I editing can result in a codon change, potentially altering the amino acid sequence of the resulting protein. This may lead to the production of a functionally distinct protein isoform. A-to-I editing also occurs in non-coding regions such as introns, untranslated regions (UTRs), and repetitive elements like LINEs and SINEs (especially Alu repeats). In these regions, editing may influence splicing, RNA stability, nuclear retention, and other aspects of RNA processing.
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