<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>5(1)</volume><submitter>Coleman SK</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Specific delivery to synapses of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors with long-tailed subunits is believed to be a key event in many forms of activity-dependent changes in synaptic strength. GluA1, the best characterized long-tailed AMPA receptor subunit, contains a C-terminal class I PDZ binding motif, which mediates its interaction with scaffold and trafficking proteins, including synapse-associated protein 97 (SAP97). In GluA4, another long-tailed subunit implicated in synaptic plasticity, the PDZ motif is blocked by a single proline residue. This feature is highly conserved in vertebrates, whereas the closest invertebrate homologs of GluA4 have a canonical class I PDZ binding motif. In this work, we have examined the role of GluA4 in</pubmed_abstract><journal>PloS one</journal><pagination>e8715</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2806832</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions.</pubmed_title><pmcid>PMC2806832</pmcid><pubmed_authors>Keinanen K</pubmed_authors><pubmed_authors>Coleman SK</pubmed_authors><pubmed_authors>Cai C</pubmed_authors><pubmed_authors>Kalkkinen N</pubmed_authors><pubmed_authors>Korpi ER</pubmed_authors></additional><is_claimable>false</is_claimable><name>Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions.</name><description>&lt;h4>Background&lt;/h4>Specific delivery to synapses of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors with long-tailed subunits is believed to be a key event in many forms of activity-dependent changes in synaptic strength. GluA1, the best characterized long-tailed AMPA receptor subunit, contains a C-terminal class I PDZ binding motif, which mediates its interaction with scaffold and trafficking proteins, including synapse-associated protein 97 (SAP97). In GluA4, another long-tailed subunit implicated in synaptic plasticity, the PDZ motif is blocked by a single proline residue. This feature is highly conserved in vertebrates, whereas the closest invertebrate homologs of GluA4 have a canonical class I PDZ binding motif. In this work, we have examined the role of GluA4 in</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Jan</publication><modification>2026-04-16T21:11:00.837Z</modification><creation>2019-03-26T23:07:10Z</creation></dates><accession>S-EPMC2806832</accession><cross_references><pubmed>20090852</pubmed><doi>10.1371/journal.pone.0008715</doi></cross_references></HashMap>