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Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
March 1994
March 1994
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Abstract
Calnexin is a new type of molecular chaperone that interacts with many nascent membrane
and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular
chaperones of the Hsp60, Hsp70 and Hsp90 families, and is further distinguished from
them in that it is an integral membrane protein. One of its demonstrated functions
is the retention of incorrectly or incompletely folded proteins, suggesting that calnexin
is a component of the quality control system of the endoplasmic reticulum.