Encyclopedia of Metalloproteins

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

Calnexin and Calreticulin

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_42

Synonyms

Definition

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.

Background

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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References

  1. Chevet E, Smirle J, Cameron PH et al (2010) Calnexin phosphorylation: linking cytoplasmic signalling to endoplasmic reticulum luminal functions. Semin Cell Dev Biol 21:486–490CrossRefPubMedGoogle Scholar
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  3. Jung J, Coe H, Opas M et al (2006) Calnexin: an endoplasmic reticulum integral membrane chaperone. Calcium Bind Proteins 1:67–71Google Scholar
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  6. Michalak M, Groenendyk J, Szabo E et al (2009) Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417:651–666CrossRefPubMedGoogle Scholar
  7. Rosenbaum EE, Hardie RC, Colley NJ (2006) Calnexin is essential for rhodopsin maturation, Ca2+ regulation, and photoreceptor cell survival. Neuron 49:229–241CrossRefPubMedGoogle Scholar
  8. Schrag JD, Bergeron JJ, Li Y et al (2001) The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 8:633–644CrossRefPubMedGoogle Scholar
  9. Williams DB (2006) Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119:615–623CrossRefPubMedGoogle Scholar

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