Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum
Pascal Gelebart1, Michal Opas, Marek Michalak
1Canadian Institute of Health Research Membrane Protein Research Group, Department of Biochemistry, University of Alberta, Edmonton, Alta., T6G 2H7C, Canada.
Abstract:
Calreticulin is a 46-kDa Ca2+-binding chaperone found across a diverse range of species. The protein is involved in the regulation of intracellular Ca2+ homeostasis and endoplasmic reticulum (ER) Ca2+ storage capacity. Calreticulin is also an important molecular chaperone involved in "quality control" within secretory pathways. The protein contains structurally and functionally unique domains with specialized functions. Studies on calreticulin knockout mice indicate that the protein is essential in early cardiac development. The protein also plays an important role in autoimmunity and cancer.
Related Concept Videos
Protein Folding Quality Check in the RER
Endoplasmic Reticulum
Tail-anchoring of Proteins in the ER Membrane
ER Retrieval Pathway
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Export of Misfolded Proteins out of the ER
Directing Proteins to the Rough Endoplasmic Reticulum


