Calreticulin: One protein, one gene, many functions

Marek Michalak, Elaine F. Corbett, Nasrin Mesaeli, Kimitoshi Nakamura, Michal Opas

Research output: Contribution to journalReview article

609 Citations (Scopus)


The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated and secreted proteins. The membrane is also an important site of Ca2+ storage and release. Calreticulin is a unique ER luminal resident protein. The protein affects many cellular functions, both in the ER lumen and outside of the ER environment. In the ER lumen, calreticulin performs two major functions: chaperoning and regulation of Ca2+ homoeostasis. Calreticulin is a highly versatile lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors, integrins and transporters. The protein also affects intracellular Ca2+ homoeostasis by modulation of ER Ca2+ storage and transport. Studies on the cell biology of calreticulin revealed that the ER membrane is a very dynamic intracellular compartment affecting many aspects of cell physiology.

Original languageEnglish
Pages (from-to)281-292
Number of pages12
JournalBiochemical Journal
Issue number2
Publication statusPublished - 1 Dec 1999



  • Ca homoeostasis
  • Chaperoning
  • Endoplasmic reticulum
  • Luminal resident protein
  • Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Michalak, M., Corbett, E. F., Mesaeli, N., Nakamura, K., & Opas, M. (1999). Calreticulin: One protein, one gene, many functions. Biochemical Journal, 344(2), 281-292.