| Annotated protein: | Protein cornichon homolog 3 (CNIH-3) (Cornichon family AMPA receptor auxiliary protein 3). Gene symbol: CNIH3. Taxonomy: Mus musculus (Mouse). Uniprot ID: Q6ZWS4 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ CNIH3 |
| Ontology domain: | Biological Process |
| SynGO term: | neurotransmitter receptor localization to postsynaptic specialization membrane (GO:0099645) |
| Synapse type(s): | hippocampus, glutamatergic |
| Annotated paper: | Herring BE, et al. "Cornichon proteins determine the subunit composition of synaptic AMPA receptors" Neuron. 2013 Mar 20;77(6):1083-96 PMID:23522044 |
| Figure(s): | Figures 2, 4 |
| Annotation description: | In CA1 pyramidal neurons, CNIH-3, together with CNIH-2, mediates the trafficking of GluA1-containing receptors to synapses. Fig. 3: "Deletion of CNIH-3 Selectively Depresses AMPAR Synaptic Transmission when Combined with CNIH-2 Deletion" Deletion of CNIH-3 alone had no effect on AMPAR- or NMDAR-eEPSCs (Figures 2A and 2B). Deletion of both CNIH-2 and CNIH-3 selectively reduced AMPAR-eEPSCs and to a greater extent than that seen in CNIH-2 KO mice (Figures 2C-2F). CNIH-2/-3 KO reduced mEPSC amplitudes (Figure 2G) to a similar extent observed in CNIH-2 KO (Figure 2G, I). However, mEPSC decay was faster in CNIH double KO neurons than CNIH-2 KO (Figures 2H and 2J). LTP was markedly reduced in CNIH-2/3 KO neurons compare to controls (Figure 2K). The effects on AMPAR-eEPSCs, mEPSC amplitudes, kinetics and LTP observed in CNIH-2/-3 KO mice phenocopied GluA1 KO. "These results suggest that CNIH-2 can compensate for the lack of CNIH-3, CNIH-2 is the dominant of the two isoforms, and CNIH-2 and CNIH-3 are both essential for synaptic AMPAR expression in the hippocampus." Fig. 4D: The deactivation of GluA2/A3/TARP g-8 complexes in HEK cells was twice as fast as GluA1/A2/TARP g-8 complexes and similar to the change in AMPAR deactivation kinetics measured in outside-out patches from CNIH-2 and CNIH-2/-3 KO CA1 pyramidal neurons. These results "indicate that the kinetic changes caused by the deletion of CNIH-2/-3 in neurons can be fully explained by the selective removal of the GluA1 subunit, leaving GluA2/A3/TARP g-8 complexes with faster kinetics." |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | RNAi / shRNA |
| Evidence tracking, Experiment Assay: | Whole-cell patch clamp |
| Annotator(s): | Hana Goldschmidt (ORCID:0000-0002-5676-366X) Richard Huganir (ORCID:0000-0001-9783-5183) |
| Lab: | Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA and Kavli Neuroscience Discovery Institute, Johns Hopkins University, Baltimore, MD 21205, USA |
| Additional literature: | Shows the effect of CNIH3 on intrinsic AMPAR channel properties in Xenopus oocytes and cultured cells @ PMID:19265014 CNIH-3 is expressed in hippocampus, but at a lower level than CNIH-2. @ PMID:17151600 |
| SynGO annotation ID: | 2696 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |