{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sanderson JL"],"funding":["NINDS NIH HHS"],"pagination":["109786"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8530450"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37(1)"],"pubmed_abstract":["Regulated insertion and removal of postsynaptic AMPA glutamate receptors (AMPARs) mediates hippocampal long-term potentiation (LTP) and long-term depression (LTD) synaptic plasticity underlying learning and memory. In Alzheimer's disease β-amyloid (Aβ) oligomers may impair learning and memory by altering AMPAR trafficking and LTP/LTD balance. Importantly, Ca<sup>2+</sup>-permeable AMPARs (CP-AMPARs) assembled from GluA1 subunits are excluded from hippocampal synapses basally but can be recruited rapidly during LTP and LTD to modify synaptic strength and signaling. By employing mouse knockin mutations that disrupt anchoring of the kinase PKA or phosphatase Calcineurin (CaN) to the postsynaptic scaffold protein AKAP150, we find that local AKAP-PKA signaling is required for CP-AMPAR recruitme"],"journal":["Cell reports"],"pubmed_title":["β-Amyloid disruption of LTP/LTD balance is mediated by AKAP150-anchored PKA and Calcineurin regulation of Ca<sup>2+</sup>-permeable AMPA receptors."],"pmcid":["PMC8530450"],"funding_grant_id":["R01 NS110383","R01 NS040701"],"pubmed_authors":["Sanderson JL","Freund RK","Gorski JA","Dell'Acqua ML"],"additional_accession":[]},"is_claimable":false,"name":"β-Amyloid disruption of LTP/LTD balance is mediated by AKAP150-anchored PKA and Calcineurin regulation of Ca<sup>2+</sup>-permeable AMPA receptors.","description":"Regulated insertion and removal of postsynaptic AMPA glutamate receptors (AMPARs) mediates hippocampal long-term potentiation (LTP) and long-term depression (LTD) synaptic plasticity underlying learning and memory. In Alzheimer's disease β-amyloid (Aβ) oligomers may impair learning and memory by altering AMPAR trafficking and LTP/LTD balance. Importantly, Ca<sup>2+</sup>-permeable AMPARs (CP-AMPARs) assembled from GluA1 subunits are excluded from hippocampal synapses basally but can be recruited rapidly during LTP and LTD to modify synaptic strength and signaling. By employing mouse knockin mutations that disrupt anchoring of the kinase PKA or phosphatase Calcineurin (CaN) to the postsynaptic scaffold protein AKAP150, we find that local AKAP-PKA signaling is required for CP-AMPAR recruitme","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2025-04-04T21:30:49.077Z","creation":"2025-04-04T21:30:49.077Z"},"accession":"S-EPMC8530450","cross_references":{"pubmed":["34610314"],"doi":["10.1016/j.celrep.2021.109786"]}}