{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Morise J"],"funding":["MEXT | Japan Society for the Promotion of Science","Ministry of Education, Culture, Sports, Science and Technology","MEXT | JST | Core Research for Evolutional Science and Technology"],"pagination":["5245"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6868016"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["The number and subunit compositions of AMPA receptors (AMPARs), hetero- or homotetramers composed of four subunits GluA1-4, in the synapse is carefully tuned to sustain basic synaptic activity. This enables stimulation-induced synaptic plasticity, which is central to learning and memory. The AMPAR tetramers have been widely believed to be stable from their formation in the endoplasmic reticulum until their proteolytic decomposition. However, by observing GluA1 and GluA2 at the level of single molecules, we find that the homo- and heterotetramers are metastable, instantaneously falling apart into monomers, dimers, or trimers (in 100 and 200 ms, respectively), which readily form tetramers again. In the dendritic plasma membrane, GluA1 and GluA2 monomers and dimers are far more mobile than te"],"journal":["Nature communications"],"pubmed_title":["AMPA receptors in the synapse turnover by monomer diffusion."],"pmcid":["PMC6868016"],"funding_grant_id":["24247029","23110006","16K14695","17K15090","16H06386","19H03370"],"pubmed_authors":["Morise J","Suzuki KGN","Wakazono Y","Takamiya K","Oka S","Takematsu H","Nemoto YL","Kusumi A","Kitagawa A","Tsunoyama TA"],"additional_accession":[]},"is_claimable":false,"name":"AMPA receptors in the synapse turnover by monomer diffusion.","description":"The number and subunit compositions of AMPA receptors (AMPARs), hetero- or homotetramers composed of four subunits GluA1-4, in the synapse is carefully tuned to sustain basic synaptic activity. This enables stimulation-induced synaptic plasticity, which is central to learning and memory. The AMPAR tetramers have been widely believed to be stable from their formation in the endoplasmic reticulum until their proteolytic decomposition. However, by observing GluA1 and GluA2 at the level of single molecules, we find that the homo- and heterotetramers are metastable, instantaneously falling apart into monomers, dimers, or trimers (in 100 and 200 ms, respectively), which readily form tetramers again. In the dendritic plasma membrane, GluA1 and GluA2 monomers and dimers are far more mobile than te","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Nov","modification":"2025-06-01T12:39:17.539Z","creation":"2025-06-01T12:39:17.539Z"},"accession":"S-EPMC6868016","cross_references":{"pubmed":["31748519"],"doi":["10.1038/s41467-019-13229-8"]}}