Amyloid beta oligomer binding site on synaptic receptor

The "Amyloid beta oligomer binding site on synaptic receptors" does not refer to a single molecular entity but rather describes multiple postsynaptic proteins and complexes that interact with soluble amyloid-beta (Aβ) oligomers. These interactions are central to the neurotoxic effects observed in Alzheimer's disease. Research has identified several postsynaptic targets for Aβ oligomers at excitatory glutamatergic synapses, including: * N-methyl-D-aspartate receptor (NMDA receptor) * Metabotropic glutamate receptor 5 (mGluR5) * Neuroligin 1 (NL1) * Cellular prion protein (PrPC) * α7-nicotinic acetylcholine receptor (α7-nAChR) [1] These proteins serve as candidate receptors or co-receptors mediating the deleterious actions of soluble Aβ species. Binding of Aβ oligomers leads to disruption of synapse composition, loss of memory-related surface receptors such as NMDA and EphB2, alteration in dendritic spine morphology, decreased long-term potentiation, and ultimately contributes to cognitive decline characteristic of Alzheimer's disease [2][1]. Because this term encompasses multiple distinct molecules rather than one canonical target—and because it lacks specificity—it should be considered an imprecise or incorrect entry for structured databases, though it accurately reflects an important pathophysiological concept. "Several Aβ oligomers receptors exist at the excitatory synapse... including glutamatergic receptors (NMDA and mGluR5), prion protein, neurotrophin receptor, and α7-nicotinic acetylcholine receptor." [1] "ADDLs have been shown...to interfere with mechanisms of synaptic plasticity...acting as gain-of-function ligands that attach to synapses." [2]

Other names

Amyloid-β oligomer receptorAβ oligomer binding siteADDL (Aβ-derived diffusible ligand) synaptic targetPostsynaptic Aβ binding protein