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Glutamate receptor ionotropic, kainate 2 (GluK2) is a subunit of kainate receptors, which are tetrameric ligand-gated ion channels in the ionotropic glutamate receptor family. GluK2 assembles to form functional kainate receptors which mediate excitatory neurotransmission and modulate synaptic transmission and plasticity in the central nervous system. Kainate receptors, including those containing GluK2, are critical for normal synaptic signaling and are implicated in a range of neurological and psychiatric diseases due to their role in regulating neuronal circuits. The receptor can function as a homomer or as a heteromer with other kainate receptor subunits (GluK1–5), and its activation and desensitization are finely controlled by ligand binding and allosteric modulation.
Agonists (e.g., glutamate, kainic acid, domoic acid) bind to the ligand-binding domain and open the cation-permeable channel, mediating excitatory currents. Positive allosteric modulators (e.g., BPAM344, concanavalin A) prolong activation by stabilizing the ligand-binding domain dimer and inhibiting desensitization.
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