| Annotated protein: | Glutamate receptor 1 (GluR-1) (AMPA-selective glutamate receptor 1) (GluR-A) (GluR-K1) (Glutamate receptor ionotropic, AMPA 1) (GluA1). Gene symbol: GRIA1. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: P19490 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ GRIA1 |
| Ontology domain: | Biological Process |
| SynGO term: | transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential (GO:1904315) |
| Synapse type(s): | hippocampus, glutamatergic |
| Annotated paper: | Hayashi Y, et al. "Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction" Science. 2000 Mar 24;287(5461):2262-7 PMID:10731148 |
| Figure(s): | fig 1, fig 2, fig 3, fig 4 |
| Annotation description: | To elucidate mechanisms that control and execute activity-dependent synaptic plasticity, GluA1 receptors with an electrophysiological tag were expressed in rat hippocampal neurons. Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged GluA1 into synapses. This effect was not diminished by mutating the CaMKII phosphorylation site on GluA1, but was blocked by mutating a predicted PDZ domain interaction site. These results show that LTP and CaMKII activity drive GluA1 to synapses by a mechanism that requires the association between GluA1 and a PDZ domain protein. |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | Over-expression |
| Evidence tracking, Experiment Assay: | Whole-cell patch clamp |
| Annotator(s): | Pim van Nierop (ORCID:0000-0003-0593-3443) Guus Smit (ORCID:0000-0002-2286-1587) Matthijs Verhage (ORCID:0000-0002-2514-0216) |
| Lab: | Department of Functional Genomics, Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands |
| Additional literature: | AMPA receptors are the principal mediators of excitatory synaptic transmission in the mammalian central nervous system. The subunit composition of these tetrameric receptors helps to define their functional properties, and may also influence the synaptic trafficking implicated in long-term synaptic plasticity. However, the organization of AMPAR subunits within the synapse remains unclear. Here, we use postembedding immunogold electron microscopy to study the synaptic organization of AMPAR subunits in stratum radiatum of CA1 hippocampus in the adult rat. We find that GluA1 concentrates away from the center of the synapse, extending at least 25 nm beyond the synaptic specialization; in contrast, GluA3 is uniformly distributed along the synapse, and seldom extends beyond its lateral border. The fraction of extrasynaptic GluA1 is markedly higher in small than in large synapses; no such effect is seen for GluA3. These observations imply that different kinds of AMPARs are differently trafficked to and/or anchored at the synapse. @ PMID:25524891 |
| SynGO annotation ID: | 2030 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |