Calcium binding chaperones of the endoplasmic reticulum

Gen Physiol Biophys. 2009;28 Spec No Focus:F96-F103.


The endoplasmic reticulum is a major Ca(2+) store of the cell that impacts many cellular processes within the cell. The endoplasmic reticulum has roles in lipid and sterol synthesis, protein folding, post-translational modification and secretion and these functions are affected by intraluminal endoplasmic reticulum Ca(2+). In the endoplasmic reticulum there are several Ca(2+) buffering chaperones including calreticulin, Grp94, BiP and protein disulfide isomerase. Calreticulin is one of the major Ca(2+) binding/buffering chaperones in the endoplasmic reticulum. It has a critical role in Ca(2+) signalling in the endoplasmic reticulum lumen and this has significant impacts on many Ca(2+)-dependent pathways including control of transcription during embryonic development. In addition to Ca(2+) buffering, calreticulin plays important role in the correct folding and quality control of newly synthesized glycoproteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Calcium / chemistry*
  • Calreticulin / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum Chaperone BiP
  • Gene Expression Regulation, Developmental
  • Glycoproteins / chemistry
  • Heat-Shock Proteins / metabolism
  • Humans
  • Membrane Glycoproteins / metabolism
  • Models, Biological
  • Molecular Chaperones / metabolism*
  • Transcription, Genetic


  • Calreticulin
  • Endoplasmic Reticulum Chaperone BiP
  • Glycoproteins
  • Heat-Shock Proteins
  • Membrane Glycoproteins
  • Molecular Chaperones
  • endoplasmin
  • Calcium