Aβ oligomer binding stimulates the clustering of specific neuronal receptors into aberrant pathogenic signalling platforms at the synapse. (a) Synaptic function and neural communication is maintained by the activity of postsynaptic receptors including the neuroprotective PrP^C and the NMDA and mGluR5 glutamate receptors, which modulate synaptic plasticity. In the healthy brain, the dynamic translocation of such receptors between lipid raft and nonraft domains of the plasma membrane modulates their activities; (b) in AD, the binding of Aβ oligomers at postsynaptic membranes causes the redistribution and clustering of receptors including PrP^C, NMDAR and mGluR5 into pathological signalling platforms [117]. The resulting loss of transient lateral movement and subsequently interaction with other components is proposed to cause a loss of normal functionality combined with aberrant signalling by these receptors. The dysregulation of Ca2⁺ and inhibition of synaptic long-term potentiation likely underlie the memory deficits which characterise AD. Further, the loss of PrP^C depletes neuronal protection against oxidative stress which may partially account for the neuronal death that is observed in AD brains.