Journal
BIOCHEMICAL JOURNAL
Volume 417, Issue -, Pages 651-666Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20081847
Keywords
calcium homoeostasis; calreticulin; endoplasmic reticulum (ER); protein folding; quality control
Categories
Funding
- Canadian Institutes of Health Research [53050, 15415, 15291, 363841]
- Alberta Heritage Foundation for Medical Research, Heart and Stroke Foundation of Alberta
- Heart and Stroke Foundation of Ontario [61811]
- Canadian Institutes of Health Research and Heart and Stroke Foundation of Canada Membrane Protein and Cardiovascular Disease Training Program
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Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved ill regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. The protein impacts on store-operated Ca2+ influx and influences Ca2+ dependent transcriptional pathways during embryonic development. Calreticulin is also involved in the folding of newly synthesized proteins and glycoproteins and, together with calnexin (an integral ER membrane chaperone similar to calreticulin) and ERp57 [ER protein of 57 kDa; a PDI (protein disulfide-isomerase)-like ER-resident protein], constitutes the 'calreticulin/calnexin cycle' that is responsible for folding and quality control of newly synthesized glycoproteins. In recent years, calreticulin has been implicated to play a role in many biological systems, including functions inside and outside the ER, indicating that the protein is a multi-process molecule. Regulation of Ca2+ homoeostasis and ER Ca2+ buffering by calreticulin might be the key to explain its multi-process property.
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