Topic: GluA3

A major component of Alzheimer's disease pathology is the accumulation of amyloid-β (Aβ), a peptide that is known to weaken synaptic transmission. Whereas both AMPA receptor (AMPAR) and NMDA receptor (NMDAR) currents are affected by Aβ oligomers, not all synapses are equally vulnerable to the toxic effects of Aβ. We set out to elucidate the roles of the different AMPAR and NMDAR subunits in synapse susceptibility to Aβ. Whole-cell patch clamp recordings were performed in hippocampal CA1 neurons that overexpress Aβ oligomers. Variance analysis was used to disentangle whether this decreased syna

Synaptic dysfunction in response to amyloid-beta (Aß) accumulation is increasingly recognized as a precursor of cognitive decline in Alzheimer's Disease (AD). AMPA receptors (AMPARs), the major neurotransmitter receptors in the brain, are implicated in the synaptic dysfunction observed in rodent models expressing amyloidogenic APP mutations. AMPARs are proposed to undergo aberrant trafficking, characterized by changes in their subunit composition and subcellular localization. The precise mechanisms underlying the dysregulation of AMPAR trafficking in AD remain poorly understood.Here, we apply

Traditionally, research on AMPA receptors has predominantly focused on GluA1 and GluA2 subunits. However, emerging consensus now emphasizes the pivotal role of GluA3 in specific forms of plasticity and behaviors. Though, most of the research conducted thus far has employed complete knockout animal model of GluA3-encoding gene (GRIA3) where compensatory events during neurodevelopment may obscure GluA3’s function.To better dissect GluA3's contribution to complex behaviors, we employed two in vivo mouse models of GluA3 downregulation in adult mice. First, we chronically administered autoantibodie