Annotated protein: | Protein cornichon homolog 2 (CNIH-2) (Cornichon family AMPA receptor auxiliary protein 2) (Cornichon-like protein). Gene symbol: CNIH2. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: Q5BJU5 |
antibody wiki: | |
SynGO gene info: | SynGO data @ CNIH2 |
Ontology domain: | Cellular Component |
SynGO term: | integral component of postsynaptic density membrane (GO:0099061) |
Synapse type(s): | hippocampus, glutamatergic forebrain, glutamatergic |
Annotated paper: | Kato AS, et al. "Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins" Neuron. 2010 Dec 22;68(6):1082-96 PMID:21172611 |
Figure(s): | Figure 5 |
Annotation description: | CNIH-2 is a multipass transmembrane protein highly expressed in the hippocampus which associates with synaptic and extrasynaptic AMPA receptors. Biochemical fractionation from adult rat forebrain shows CNIH-2 is concentrated in the postsynaptic density (Figure 5B). Surface biotinylation and western blot analysis of hippocampal slices demonstrates CNIH-2 is localized to the cell surface (Supplemental Figure S4). In cultured hippocampal neurons, endogenous CNIH-2 show a punctate distribution along dendrites and in dendritic spines which colocalize with GluA1 and TARPs (Figure 5E-F). CNIH-2 antibody: The authors generated antibodies to CNIH-2 and demonstrate its specificity by western blot analysis of lysates from (1) CNIH-2 transfected HEK cells and (2) adult mouse hippocampal tissue (Figure 5A) and immunostaining of CNIH-2 shRNA transfected neurons (Supplemental Figure S6). 8/12/2017 Pim - Integration of the biochemical enrichment in the PSD fractions, colocalization with GluA1 and TARP at the tip of dendritic spines, and the localization to the cell surface together justify term 'integral component of postsynaptic density membrane (GO:0099061)'. |
Evidence tracking, Biological System: | Intact tissue Cultured neurons |
Evidence tracking, Protein Targeting: | Antibody (detection) |
Evidence tracking, Experiment Assay: | Confocal Western blot Biochemical fractionation (generic) |
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: | Identification of CNIH-2 and CNIH-3 as proteins that coassemble with AMPA receptors at excitatory synapses in the adult rat hippocampus. Immuno-EM with a pan-CNIH antibody (CNIH-2/-3) shows CNIHs localize to the postsynaptic density of asymmetric synapses on dendritic spines in CA1 pyramidal neurons (Figure 3). @ PMID:19265014 |
SynGO annotation ID: | 2188 |
Dataset release (version): | 20231201 |
View annotation as GO-CAM model: |