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:Gene Ontology