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Protein cornichon homolog 1 (CNIH1) is an evolutionarily conserved transmembrane protein belonging to the cornichon family that acts primarily as a COPII cargo receptor and an auxiliary protein for AMPA-type ionotropic glutamate receptors (AMPARs)[2][3]. In mammalian cells, CNIH1 is localized to the endoplasmic reticulum and Golgi apparatus, where it facilitates the exit and trafficking of select membrane proteins through the secretory pathway, most notably TGFα in humans and AMPA receptors in neurons. Unlike other cornichon family members (CNIH2, CNIH3), which robustly regulate AMPA receptor gating and trafficking, CNIH1 can bind to these receptors but is inefficient at modulating their channel properties[2][3]. Cornichon homologs in plants and yeast have similar functional roles, mediating the ER export of ion transporters. No clinical drugs are known to directly target or interact with CNIH1, and it is not currently used as a biomarker. Its dysfunction or altered expression could theoretically impact synaptic function or membrane protein localization but has not been definitively linked to any human disease[2][3][1].
Not applicable; no drugs are currently known to bind or modulate CNIH1 directly.
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