{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pandya NJ"],"funding":["European Research Council","Dutch Research Council (NWO)","Marie Curie"],"pagination":["1218-1230"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6088136"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(5)"],"pubmed_abstract":["Lateral diffusion on the neuronal plasma membrane of the AMPA-type glutamate receptor (AMPAR) serves an important role in synaptic plasticity. We investigated the role of the secreted glycoprotein Noelin1 (Olfactomedin-1 or Pancortin) in AMPAR lateral mobility and its dependence on the extracellular matrix (ECM). We found that Noelin1 interacts with the AMPAR with high affinity, however, without affecting rise- and decay time and desensitization properties. Noelin1 co-localizes with synaptic and extra-synaptic AMPARs and is expressed at synapses in an activity-dependent manner. Single-particle tracking shows that Noelin1 reduces lateral mobility of both synaptic and extra-synaptic GluA1-containing receptors and affects short-term plasticity. While the ECM does not constrain the synaptic po"],"journal":["Cell reports"],"pubmed_title":["Noelin1 Affects Lateral Mobility of Synaptic AMPA Receptors."],"pmcid":["PMC6088136"],"funding_grant_id":["016.150.673","281443","MEST-ITN-2"],"pubmed_authors":["Lodder JC","Heine M","Mansvelder HD","Frischknecht R","Gonzalez-Lozano MA","Babai N","Seeger C","Li KW","Pandya NJ","Gouwenberg Y","Mack V","Spijker S","Danielson UH","Smit AB"],"additional_accession":[]},"is_claimable":false,"name":"Noelin1 Affects Lateral Mobility of Synaptic AMPA Receptors.","description":"Lateral diffusion on the neuronal plasma membrane of the AMPA-type glutamate receptor (AMPAR) serves an important role in synaptic plasticity. We investigated the role of the secreted glycoprotein Noelin1 (Olfactomedin-1 or Pancortin) in AMPAR lateral mobility and its dependence on the extracellular matrix (ECM). We found that Noelin1 interacts with the AMPAR with high affinity, however, without affecting rise- and decay time and desensitization properties. Noelin1 co-localizes with synaptic and extra-synaptic AMPARs and is expressed at synapses in an activity-dependent manner. Single-particle tracking shows that Noelin1 reduces lateral mobility of both synaptic and extra-synaptic GluA1-containing receptors and affects short-term plasticity. While the ECM does not constrain the synaptic po","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jul","modification":"2026-05-02T08:56:54.158Z","creation":"2025-05-18T12:18:48.206Z"},"accession":"S-EPMC6088136","cross_references":{"pubmed":["30067977"],"doi":["10.1016/j.celrep.2018.06.102"]}}