Calnexin (CANX)

Calnexin (CANX) is a type 1 integral membrane protein of the endoplasmic reticulum (ER) that serves as a molecular chaperone and lectin. Its main function is to assist in the folding, quality control, and ER retention of newly synthesized glycoproteins by binding monoglucosylated N-glycans. Calnexin works as part of the calnexin/calreticulin cycle, ensuring only properly folded and assembled glycoproteins proceed through the secretory pathway, while misfolded proteins are retained and targeted for degradation if necessary. Calnexin is also crucial for proper assembly of the major histocompatibility complex class I, participating in immune surveillance. Its dysfunction is associated with neurodegenerative diseases (such as Charcot-Marie-Tooth disease and multiple sclerosis), neuroinflammation, and disorders of protein aggregation and degradation. While emerging as a potential research target for neurodegeneration and viral infection, it is not currently the direct molecular target of any approved therapeutic drugs.

Other names

CANXCNXIP90P90Major histocompatibility complex class I antigen-binding protein p88p90Epididymis secretory sperm binding proteinCalnexin, epididymis secretory sperm binding protein

Not applicable for clinical drugs as above, but for research contexts: Modulation of calnexin's chaperone cycle may potentially impact the folding and ER retention of glycoproteins, assembly of MHC I, and cellular stress responses.