{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["5(1)"],"submitter":["Coleman SK"],"pubmed_abstract":["<h4>Background</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"],"journal":["PloS one"],"pagination":["e8715"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2806832"],"repository":["biostudies-literature"],"pubmed_title":["Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions."],"pmcid":["PMC2806832"],"pubmed_authors":["Keinanen K","Coleman SK","Cai C","Kalkkinen N","Korpi ER"],"additional_accession":[]},"is_claimable":false,"name":"Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions.","description":"<h4>Background</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","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jan","modification":"2026-04-16T21:11:00.837Z","creation":"2019-03-26T23:07:10Z"},"accession":"S-EPMC2806832","cross_references":{"pubmed":["20090852"],"doi":["10.1371/journal.pone.0008715"]}}