Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
- PMID: 19133842
- DOI: 10.1042/BJ20081847
Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
Abstract
Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved in 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.
Similar articles
-
Calcium binding chaperones of the endoplasmic reticulum.Gen Physiol Biophys. 2009;28 Spec No Focus:F96-F103. Gen Physiol Biophys. 2009. PMID: 20093733 Review.
-
Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum.Int J Biochem Cell Biol. 2005 Feb;37(2):260-6. doi: 10.1016/j.biocel.2004.02.030. Int J Biochem Cell Biol. 2005. PMID: 15474971 Review.
-
Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum.J Cell Sci. 2006 Feb 15;119(Pt 4):615-23. doi: 10.1242/jcs.02856. J Cell Sci. 2006. PMID: 16467570 Review.
-
Protein folding and quality control in the endoplasmic reticulum.Curr Opin Cell Biol. 2004 Aug;16(4):343-9. doi: 10.1016/j.ceb.2004.06.012. Curr Opin Cell Biol. 2004. PMID: 15261665 Review.
-
Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding.Cell Biochem Biophys. 2003;39(3):223-47. doi: 10.1385/CBB:39:3:223. Cell Biochem Biophys. 2003. PMID: 14716078 Review.
Cited by
-
Identifying natural substrates for dipeptidyl peptidases 8 and 9 using terminal amine isotopic labeling of substrates (TAILS) reveals in vivo roles in cellular homeostasis and energy metabolism.J Biol Chem. 2013 May 17;288(20):13936-13949. doi: 10.1074/jbc.M112.445841. Epub 2013 Mar 21. J Biol Chem. 2013. PMID: 23519473 Free PMC article.
-
Calreticulin translocation aggravates endoplasmic reticulum stress-associated apoptosis during cardiomyocyte hypoxia/reoxygenation.Chin Med J (Engl). 2015 Feb 5;128(3):353-60. doi: 10.4103/0366-6999.150103. Chin Med J (Engl). 2015. PMID: 25635431 Free PMC article.
-
Recent advances in understanding myelofibrosis and essential thrombocythemia.F1000Res. 2016 Apr 19;5:F1000 Faculty Rev-700. doi: 10.12688/f1000research.8081.1. eCollection 2016. F1000Res. 2016. PMID: 27134742 Free PMC article. Review.
-
A novel signalling screen demonstrates that CALR mutations activate essential MAPK signalling and facilitate megakaryocyte differentiation.Leukemia. 2017 Apr;31(4):934-944. doi: 10.1038/leu.2016.280. Epub 2016 Oct 14. Leukemia. 2017. PMID: 27740635 Free PMC article.
-
Cold-induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice.EMBO J. 2023 Jan 4;42(1):e110518. doi: 10.15252/embj.2021110518. Epub 2022 Nov 7. EMBO J. 2023. PMID: 36341575 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Research Materials
Miscellaneous
