Calreticulin: Not Just Another Calcium-Binding Protein

Mol Cell Biochem. 1994 Jun 15;135(1):71-8. doi: 10.1007/BF00925962.

Abstract

In this paper we review some of the rapidly expanding information about calreticulin, a Ca(2+)-binding/storage protein of the endoplasmic reticulum. The emphasis is placed on the structure and function of calreticulin. We believe that calreticulin is a multifunctional Ca(2+)-binding protein and that distinct functional properties of the protein may be localized to each of the three structural domains of calreticulin. Most evidence indicates that calreticulin is a resident endoplasmic reticulum protein. However, it can also be found outside of the endoplasmic reticulum compartment, i.e. in the nuclear envelope, in the nucleus, in the cytotoxic granules in T-lymphocytes and in acrosomal vesicles of sperm cells. The evidence reviewed here clearly suggests that calreticulin has other functions in addition to its role as a Ca2+ storage protein in the endoplasmic reticulum.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Autoantigens / chemistry
  • Autoantigens / physiology
  • Biological Transport / physiology
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / physiology*
  • Calreticulin
  • Endoplasmic Reticulum / metabolism*
  • Humans
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Ribonucleoproteins / chemistry
  • Ribonucleoproteins / physiology*
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship

Substances

  • Autoantigens
  • Calcium-Binding Proteins
  • Calreticulin
  • Ribonucleoproteins