Glur2-Subunit (Ser880) (GRIA2) Antibody – Rabbit Polyclonal

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), and function as ligand-activated cation channels. These channels are assembled from 4 related subunits, Gria1-4. The subunit encoded by this gene (Gria2) is subject to RNA editing (Q/R and R/G), which is thought to render the channels impermeable to Ca(2+), and to affect the kinetic aspects of these channels in rat brain. Alternative splicing, resulting in transcript variants encoding different isoforms (flip and flop), has been noted for this gene. [provided by RefSeq, Jul 2008]

Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Ref.4 Ref.19 Ref.20 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36

Subunit structure: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4

By similarity. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with NSF via its C-terminus. Interacts with CACNG2, PRKCABP and GRIP2. Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ domain)

By similarity. Interacts with GRIA1 and SYNDIG1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes

By similarity. Interacts with LRFN1. Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5. Ref.6 Ref.7 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.26 Ref.34 Ref.35

Subcellular location: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Ref.6 Ref.12 Ref.14 Ref.19

Tissue specificity: Detected in forebrain. Detected in dendrites of neuronal cells. Ref.6 Ref.12 Ref.13

Developmental stage: Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 8 to 14 day old animals. Detected at intermediate levels at day 42 (at protein level). Ref.12

Domain: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression

By similarity.

Post-translational modification: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis

By similarity.

Miscellaneous: The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.

Sequence similarities: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA2 subfamily. [View classification]

RNA editing: Edited at position 607.Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions

By similarity. Ref.5