Calnexin: a membrane-bound chaperone of the endoplasmic reticulum

Trends Biochem Sci. 1994 Mar;19(3):124-8. doi: 10.1016/0968-0004(94)90205-4.


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.

Publication types

  • Review

MeSH terms

  • Calcium-Binding Proteins / metabolism*
  • Calnexin
  • Endoplasmic Reticulum / metabolism*
  • Membrane Proteins / metabolism*
  • Structure-Activity Relationship


  • Calcium-Binding Proteins
  • Membrane Proteins
  • Calnexin