<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Pandya NJ</submitter><funding>European Research Council</funding><funding>Dutch Research Council (NWO)</funding><funding>Marie Curie</funding><pagination>1218-1230</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6088136</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(5)</volume><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</pubmed_abstract><journal>Cell reports</journal><pubmed_title>Noelin1 Affects Lateral Mobility of Synaptic AMPA Receptors.</pubmed_title><pmcid>PMC6088136</pmcid><funding_grant_id>016.150.673</funding_grant_id><funding_grant_id>281443</funding_grant_id><funding_grant_id>MEST-ITN-2</funding_grant_id><pubmed_authors>Lodder JC</pubmed_authors><pubmed_authors>Heine M</pubmed_authors><pubmed_authors>Mansvelder HD</pubmed_authors><pubmed_authors>Frischknecht R</pubmed_authors><pubmed_authors>Gonzalez-Lozano MA</pubmed_authors><pubmed_authors>Babai N</pubmed_authors><pubmed_authors>Seeger C</pubmed_authors><pubmed_authors>Li KW</pubmed_authors><pubmed_authors>Pandya NJ</pubmed_authors><pubmed_authors>Gouwenberg Y</pubmed_authors><pubmed_authors>Mack V</pubmed_authors><pubmed_authors>Spijker S</pubmed_authors><pubmed_authors>Danielson UH</pubmed_authors><pubmed_authors>Smit AB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Noelin1 Affects Lateral Mobility of Synaptic AMPA Receptors.</name><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</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Jul</publication><modification>2026-05-02T08:56:54.158Z</modification><creation>2025-05-18T12:18:48.206Z</creation></dates><accession>S-EPMC6088136</accession><cross_references><pubmed>30067977</pubmed><doi>10.1016/j.celrep.2018.06.102</doi></cross_references></HashMap>