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Biochem J. 1999 Dec 1;344 Pt 2:281-92.

Calreticulin: one protein, one gene, many functions.

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  • 1MRC Group in Molecular Biology of Membranes, Department of Biochemistry, University of Alberta, 3-56 Medical Sciences Building, Edmonton, Alberta, Canada T6G 2H7. Marek.Michalak@ualberta.ca

Abstract

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 Ca(2+) 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 Ca(2+) 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 Ca(2+) homoeostasis by modulation of ER Ca(2+) 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.

PMID:
10567207
[PubMed - indexed for MEDLINE]
PMCID:
PMC1220642
Free PMC Article
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