CNIH2,3 bind GRIA1

Stable Identifier
Homo sapiens
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CNIH2 and 3 are members of the ERV14 family of transmembrane proteins with a role in chaperoning cargo out of the ER (reviewed in Dancourt and Barlowe, 2010). CNIH2 and 3 bind to components of the AMPA-type glutamate receptor complex, including GRIA1 in the ER and facilitate their trafficking to the plasma membrane. CNIH2 and 3 may play additional roles at the cell surface modulating the function of the channels (Shi et al, 2010; Schwenk et al, 2009).

Literature References
PubMed ID Title Journal Year
20533886 Protein sorting receptors in the early secretory pathway

Dancourt, J, Barlowe, C

Annu. Rev. Biochem. 2010
19265014 Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors

Zolles, G, Heimrich, B, Schulte, U, Bildl, W, Schwenk, J, Fakler, B, Kulik, A, Klöcker, N, Jonas, P, Chisaka, O, Harmel, N

Science 2009
20805473 Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating

Roche, KW, Suh, YH, Nicoll, RA, Isozaki, K, Milstein, AD, Shi, Y, Schmid, SM

Proc. Natl. Acad. Sci. U.S.A. 2010
Orthologous Events
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