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Revision as of 23:17, 6 April 2010

This family of GBPs is widespread in evolution and plays a key role in ER quality control (16-24)[1][2][3][4][5][6][7][8][9]. Work in a number of laboratories suggests that calreticulin plays a role as a molecular chaperone acting in consort with components of the oligosaccharide processing machinery to ensure ER quality control by limiting the mobility of improperly folded proteins (17-19, 24-26)[2][3][4][9][10][11]. Calreticulin has also been suggested to be a component of the peptide loading complex where it interacts with other ER resident proteins to produce class-I major histocompatibility complex (MHC-1) molecules (26-28)[11][12][13]. Other ER chaperones have been suggested to have “lectinic” properties including calnexin [1], but calreticulin is the best studied of this family.


CFG Participating Investigators contributing to the understanding of this paradigm

  • CFG Participating Investigators (PIs) working on calreticulin include: John Hanover, Jamie Rossjohn, Bingdong Sha
  • Non-PIs researchers actively pursuing the ER lectins include: Ari Helenius
  • Non-PIs focused on ER stress include: Mark Lehrman, Kelly Moreman

Progress toward understanding this GBP paradigm

Carbohydrate ligands

Cellular expression


Biological roles of GBP-ligand interaction

CFG resources used in investigations

The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for calreticulin.

Glycan profiling

Glycogene microarray

Knockout mouse lines

Glycan array

Human recombinant calreticulin was screened on the CFG glycan array (data).

Related GBPs



  1. 1.0 1.1 Ellgaard, L. and Frickel, E. M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39, 223-247 (2003)
  2. 2.0 2.1 Jorgensen, M. M., Bross, P. and Gregersen, N. Protein quality control in the endoplasmic reticulum. APMIS Suppl 86-91 (2003)
  3. 3.0 3.1 Ellgaard, L. and Helenius, A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4, 181-191 (2003)
  4. 4.0 4.1 Helenius, A. and Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049 (2004)
  5. Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M. and Helenius, A. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13, 125-135 (2004)
  6. Deprez, P., Gautschi, M. and Helenius, A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell 19, 183-195 (2005)
  7. Wu, J. C., Liang, Z. Q. and Qin, Z. H. Quality control system of the endoplasmic reticulum and related diseases. Acta Biochim Biophys Sin (Shanghai) 38, 219-226 (2006)
  8. Caramelo, J. J. and Parodi, A. J. Getting in and out from calnexin/calreticulin cycles. J Biol Chem 283, 10221-10225 (2008)
  9. 9.0 9.1 Michalak, M., Groenendyk, J., Szabo, E., Gold, L. I. and Opas, M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417, 651-666 (2009)
  10. Gelebart, P., Opas, M. and Michalak, M. Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37, 260-266 (2005)
  11. 11.0 11.1 Wearsch, P. A. and Cresswell, P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol 20, 624-631 (2008)
  12. Raghavan, M., Del Cid, N., Rizvi, S. M. and Peters, L. R. MHC class I assembly: out and about. Trends Immunol 29, 436-443 (2008)
  13. Howe, C., Garstka, M., Al-Balushi, M., Ghanem, E., Antoniou, A. N., Fritzsche, S., Jankevicius, G., Kontouli, N., Schneeweiss, C., Williams, A., Elliott, T. and Springer, S. Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. EMBO J 28, 3730-3744 (2009)


The CFG is grateful to the following PIs for their contributions to this wiki page: John Hanover

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