CNIH3 = Rat, mouse, human – 11/13 amino acid residues identical.
- Mouse and rat brain lysates (1:200-1:1000).
- Western blot analysis of mouse (lanes 1 and 3) and rat (lanes 2 and 4) brain lysates:1,2. Anti-CNIH2/3 (extracellular) Antibody (#AGC-047), (1:200).
3,4. Anti-CNIH2/3 (extracellular) Antibody, preincubated with CNIH2/3 (extracellular) Blocking Peptide (#BLP-GC047).
Cornichon homologs (CNIHs) are a family of AMPA-type glutamate receptor (AMPAR) auxiliary subunits that modulate AMPAR ion channel function and trafficking. Cornichon 2 and 3 (CNIH2/3) are responsible for controlling the export of AMPARs from the endoplasmic reticulum and associate with synaptic AMPARs to modulate channel kinetics1,2.
CNIHs are small proteins with three transmembrane domains that directly binds to AMPARs. Overexpression CNIHs and AMPA receptors causes their localization to the Golgi apparatus3.
CNIH and TARP both compete for the binding to AMPAR subunits GluA2, GluA3, and GluA4 subunits suggesting both proteins bind to the same site. CNIH2/3 binding to AMPARs is dependent on AMPAR subunit composition and TARPs3,4.
CNIH2/3 knock out mice shows alterations in synaptic content of GluA1-containing AMPARs, resulting in a reduction in AMPAR-mediated transmission and long-term potentiation2.