Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Calnexin and Calreticulin

  • Elzbieta DudekEmail author
  • Marek Michalak
Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_42



Both of these proteins are present in endoplasmic reticulum that bind to misfolded proteins and assist in their folding and posttranslational modification. Calnexin is an integral membrane protein and endoplasmic reticulum–associated molecular chaperone. Calreticulin is known as a multifunctional Ca2+-binding/buffering endoplasmic reticulum resident chaperone. The protein is responsible for buffering of over 50% of endoplasmic reticulum luminal Ca2+ and assisting in folding of newly synthesized glycoproteins.


The endoplasmic reticulum (ER) is a multifunctional organelle responsible for many vital processes in the cell including the synthesis, intracellular transport, and quality control of membrane-associated and secreted proteins; lipid and steroid synthesis; Ca2+signaling and homeostasis; communication with other intracellular organelles including the mitochondria and plasma membrane and ER...

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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of BiochemistryUniversity of AlbertaEdmontonCanada
  2. 2.Faculty of Medicine and DentistryUniversity of AlbertaEdmontonCanada