Calreticulin: Endoplasmic reticulum Ca
Journal
Journal of cellular and molecular medicine
ISSN: 1582-4934
Titre abrégé: J Cell Mol Med
Pays: England
ID NLM: 101083777
Informations de publication
Date de publication:
09 Jul 2023
09 Jul 2023
Historique:
revised:
21
06
2023
received:
21
04
2023
accepted:
27
06
2023
medline:
10
7
2023
pubmed:
10
7
2023
entrez:
10
7
2023
Statut:
aheadofprint
Résumé
Endoplasmic reticulum (ER) luminal Ca
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : CIHR
ID : PS 168843
Pays : Canada
Organisme : Multiple Sclerosis Society
Pays : United Kingdom
Informations de copyright
© 2023 The Author. Journal of Cellular and Molecular Medicine published by Foundation for Cellular and Molecular Medicine and John Wiley & Sons Ltd.
Références
Ostwald TJ, MacLennan DH, Dorrington KJ. Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum. J Biol Chem. 1974;249:5867-5871.
Michalak M, Opas M. Endoplasmic and sarcoplasmic reticulum in the heart. Trends Cell Biol. 2009;19(6):253-259. doi:10.1016/j.tcb.2009.03.006
Fliegel L, Burns K, Opas M, Michalak M. The high-affinity calcium binding protein of sarcoplasmic reticulum. Tissue distribution, and homology with calregulin. Biochim Biophys Acta. 1989;982:1-8.
Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem. 1989;264:21522-21528.
Michalak M, Milner RE. Calreticulin: a functional analogue of calsequestrin. Basic App Myol. 1991;1:121-128.
Michalak M, Baksh S, Opas M. Identification and immunolocalization of calreticulin in pancreatic cells: no evidence for "calciosomes". Exp Cell Res. 1991;197:91-99.
Milner RE, Baksh S, Shemanko C, et al. Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. J Biol Chem. 1991;266:7155-7165.
Smith MJ, Koch GL. Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J. 1989;8(12):3581-3586.
Lewis MJ, Sweet DJ, Pelham HR. The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell. 1990;61(7):1359-1363.
Lewis MJ, Pelham HR. A human homologue of the yeast HDEL receptor. Nature. 1990;348(6297):162-163.
Semenza JC, Hardwick KG, Dean N, Pelham HR. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell. 1990;61(7):1349-1357. doi:10.1016/0092-8674(90)90698-e
Krebs J, Agellon LB, Michalak M. Ca2+ homeostasis and endoplasmic reticulum (ER) stress: an integrated view of calcium signaling. Biochem Biophys Res Commun. 2015;460(1):114-121. doi:10.1016/j.bbrc.2015.02.004
Berridge MJ. The inositol trisphosphate/calcium signaling pathway in health and disease. Physiol Rev. 2016;96(4):1261-1296. doi:10.1152/physrev.00006.2016
Putney JW. Forms and functions of store-operated calcium entry mediators, STIM and Orai. Adv Biol Regul. 2018;68:88-96. doi:10.1016/j.jbior.2017.11.006
Rizzuto R, Pozzan T. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev. 2006;86(1):369-408. doi:10.1152/physrev.00004.2005
Carafoli E, Krebs J. Why calcium? How calcium became the best communicator. J Biol Chem. 2016;291(40):20849-20857. doi:10.1074/jbc.R116.735894
Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J. 2009;417(3):651-666. doi:10.1042/BJ20081847
Dai N, Groenendyk J, Michalak M. Binding Proteins | Ca2+ Binding/Buffering Proteins: ER Luminal Proteins. Encycl Biol Chem. 2021;3:534-546. doi:10.1016/B978-0-12-809633-8.21377-0
Wang WA, Agellon LB, Michalak M. Organellar calcium handling in the cellular reticular network. Cold Spring Harb Perspect Biol. 2019;11(12):a038265. 10.1101/cshperspect.a038265
Hebert DN, Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev. 2007;87(4):1377-1408.
Tannous A, Pisoni GB, Hebert DN, Molinari M. N-linked sugar-regulated protein folding and quality control in the ER. Semin Cell Dev Biol. 2015;41:79-89. doi:10.1016/j.semcdb.2014.12.001
Maattanen P, Gehring K, Bergeron JJ, Thomas DY. Protein quality control in the ER: the recognition of misfolded proteins. Semin Cell Dev Biol. 2010;21(5):500-511. doi:10.1016/j.semcdb.2010.03.006
Maattanen P, Kozlov G, Gehring K, Thomas DY. ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations. Biochem Cell Biol. 2006;84(6):881-889. doi:10.1139/o06-186
Kozlov G, Maattanen P, Thomas DY, Gehring K. A structural overview of the PDI family of proteins. FEBS J. 2010;277(19):3924-3936. doi:10.1111/j.1742-4658.2010.07793.x
Chevet E, Smirle J, Cameron PH, Thomas DY, Bergeron JJ. Calnexin phosphorylation: linking cytoplasmic signalling to endoplasmic reticulum lumenal functions. Semin Cell Dev Biol. 2010;21(5):486-490. doi:10.1016/j.semcdb.2009.12.005
Cahu X, Constantinescu SN. Oncogenic drivers in myeloproliferative neoplasms: from JAK2 to Calreticulin mutations. Curr Hematol Malig rep. 2015;10(4):335-343. doi:10.1007/s11899-015-0278-x
Smirle J, Au CE, Jain M, Dejgaard K, Nilsson T, Bergeron J. Cell biology of the endoplasmic reticulum and the Golgi apparatus through proteomics. Cold Spring Harb Perspect Biol. 2013;5(1):a015073. doi:10.1101/cshperspect.a015073
Fucikova J, Spisek R, Kroemer G, Galluzzi L. Calreticulin and cancer. Cell Res. 2021;31(1):5-16. doi:10.1038/s41422-020-0383-9
How J, Hobbs GS, Mullally A. Mutant calreticulin in myeloproliferative neoplasms. Blood. 2019;134(25):2242-2248. doi:10.1182/blood.2019000622
Gold LI, Eggleton P, Sweetwyne MT, et al. Calreticulin: non-endoplasmic reticulum functions in physiology and disease. FASEB J. 2010;24(3):665-683. doi:10.1096/fj.09-145482
Pizzo P, Pozzan T. Mitochondria-endoplasmic reticulum choreography: structure and signaling dynamics. Trends Cell Biol. 2007;17(10):511-517. doi:10.1016/j.tcb.2007.07.011
Johnson JD, Chang JP. Function- and agonist-specific Ca2+ signalling: the requirement for and mechanism of spatial and temporal complexity in Ca2+ signals. Biochem Cell Biol. 2000;78(3):217-240.
Reddish FN, Miller CL, Gorkhali R, Yang JJ. Calcium dynamics mediated by the endoplasmic/sarcoplasmic reticulum and related diseases. Int J Mol Sci. 2017;18(5):1024. doi:10.3390/ijms18051024
Groenendyk J, Agellon LB, Michalak M. Calcium signaling and endoplasmic reticulum stress. Int Rev Cell Mol Biol. 2021;363:1-20. doi:10.1016/bs.ircmb.2021.03.003
Lu YC, Weng WC, Lee H. Functional roles of calreticulin in cancer biology. Biomed Res Int. 2015;2015:526524. doi:10.1155/2015/526524
Varricchio L, Falchi M, Dall'Ora M, et al. Calreticulin: challenges posed by the intrinsically disordered nature of Calreticulin to the study of its function. Front Cell Dev Biol. 2017;5:96. doi:10.3389/fcell.2017.00096
Jia XY, He LH, Jing RL, Li RZ. Calreticulin: conserved protein and diverse functions in plants. Physiol Plant. 2009;136(2):127-138. doi:10.1111/j.1399-3054.2009.1223.x
Kozlov G, Gehring K. Calnexin cycle - structural features of the ER chaperone system. FEBS J. 2020;287(20):4322-4340. doi:10.1111/febs.15330
Harada Y, Ohkawa Y, Maeda K, Taniguchi N. Glycan quality control in and out of the endoplasmic reticulum of mammalian cells. FEBS J. 2021;289(22):7147-7162. doi:10.1111/febs.16185
Braakman I, Hebert DN. Protein folding in the endoplasmic reticulum. Cold Spring Harb Perspect Biol. 2013;5(5):a013201. 10.1101/cshperspect.a013201
Eisner DA, Caldwell JL, Kistamas K, Trafford AW. Calcium and excitation-contraction coupling in the heart. Circ Res. 2017;121(2):181-195. doi:10.1161/CIRCRESAHA.117.310230
Jiang Y, Tao Z, Chen H, Xia S. Endoplasmic reticulum quality control in immune cells. Front Cell Dev Biol. 2021;9:740653. doi:10.3389/fcell.2021.740653
Groenendyk J, Agellon LB, Michalak M. Coping with endoplasmic reticulum stress in the cardiovascular system. Annu Rev Physiol. 2013;75:49-67. doi:10.1146/annurev-physiol-030212-183707
Hetz C, Zhang K, Kaufman RJ. Mechanisms, regulation and functions of the unfolded protein response. Nat Rev Mol Cell Biol. 2020;21(8):421-438. doi:10.1038/s41580-020-0250-z
Kielbik M, Szulc-Kielbik I, Klink M. Calreticulin-multifunctional chaperone in immunogenic cell death: potential significance as a prognostic biomarker in ovarian cancer patients. Cells. 2021;10(1):130. doi:10.3390/cells10010130
Padovani C, Jevtic P, Rape M. Quality control of protein complex composition. Mol Cell. 2022;82:1439-1450. doi:10.1016/j.molcel.2022.02.029
Verkhratsky A. Calcium and cell death. Subcell Biochem. 2007;45:465-480. doi:10.1007/978-1-4020-6191-2_17
Wei C, Wang X, Zheng M, Cheng H. Calcium gradients underlying cell migration. Curr Opin Cell Biol. 2012;24(2):254-261. doi:10.1016/j.ceb.2011.12.002
Hernandez-Ochoa EO, Pratt SJP, Lovering RM, Schneider MF. Critical role of intracellular RyR1 calcium release channels in skeletal muscle function and disease. Front Physiol. 2015;6:420. doi:10.3389/fphys.2015.00420
Qiu R, Lewis RS. Structural features of STIM and Orai underlying store-operated calcium entry. Curr Opin Cell Biol. 2019;57:90-98. doi:10.1016/j.ceb.2018.12.012
Verkhratsky A. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol Rev. 2005;85(1):201-279. doi:10.1152/physrev.00004.2004
Persson S, Rosenquist M, Sommarin M. Identification of a novel calreticulin isoform (Crt2) in human and mouse. Gene. 2002;297(1-2):151-158. doi:10.1016/s0378-1119(02)00880-6
Persson S, Rosenquist M, Svensson K, Galvao R, Boss WF, Sommarin M. Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants. Plant Physiol. 2003;133(3):1385-1396. doi:10.1104/pp.103.024943
Xiang Y, Lu YH, Song M, et al. Overexpression of a Triticum aestivum Calreticulin gene (TaCRT1) improves salinity tolerance in tobacco. PLoS One. 2015;10(10):e0140591. doi:10.1371/journal.pone.0140591
Joshi R, Paul M, Kumar A, Pandey D. Role of calreticulin in biotic and abiotic stress signalling and tolerance mechanisms in plants. Gene. 2019;714:144004. doi:10.1016/j.gene.2019.144004
McCauliffe DP, Yang YS, Wilson J, Sontheimer RD, Capra JD. The 5′-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J Biol Chem. 1992;267:2557-2562.
Waser M, Mesaeli N, Spencer C, Michalak M. Regulation of calreticulin gene expression by calcium. J Cell Biol. 1997;138:547-557.
Qiu Y, Michalak M. Transcriptional control of the calreticulin gene in health and disease. Int J Biochem Cell Biol. 2009;41(3):531-538. doi:10.1016/j.biocel.2008.06.020
Paskevicius T, Farraj RA, Michalak M, Agellon LB. Calnexin, more than just a molecular chaperone. Cell. 2023;12(3):403.
Tjoelker LW, Seyfried CE, Eddy RL Jr, et al. Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry. 1994;33(11):3229-3236.
Muller-Taubenberger A, Lupas AN, Li H, Ecke M, Simmeth E, Gerisch G. Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis. EMBO J. 2001;20(23):6772-6782. doi:10.1093/emboj/20.23.6772
Kozlov G, Pocanschi CL, Rosenauer A, et al. Structural basis of carbohydrate recognition by calreticulin. J Biol Chem. 2010;285(49):38612-38620. doi:10.1074/jbc.M110.168294
Chouquet A, Paidassi H, Ling WL, et al. X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism. PLoS One. 2011;6(3):e17886. doi:10.1371/journal.pone.0017886
Ellgaard L, Riek R, Herrmann T, et al. NMR structure of the calreticulin P-domain. Proc Natl Acad Sci U S A. 2001;98(6):3133-3138. doi:10.1073/pnas.051630098
Blees A, Januliene D, Hofmann T, et al. Structure of the human MHC-I peptide-loading complex. Nature. 2017;551(7681):525-528. doi:10.1038/nature24627
Martin V, Groenendyk J, Steiner SS, et al. Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin. J Biol Chem. 2006;281(4):2338-2346.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci U S A. 2002;99:1954-1959.
Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. Localization of the lectin, ERp57 binding, and polypeptide binding sites of Calnexin and Calreticulin. J Biol Chem. 2002;277(33):29686-29697.
Pallero MA, Elzie CA, Chen J, Mosher DF, Murphy-Ullrich JE. Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis. FASEB J. 2008;22(11):3968-3979. doi:10.1096/fj.07-104802
Yang H, Ahmad ZA, Song Y. Molecular insight for the role of key residues of calreticulin in its binding activities: a computational study. Comput Biol Chem. 2020;85:107228. doi:10.1016/j.compbiolchem.2020.107228
Ciplys E, Paskevicius T, Zitkus E, et al. Mapping human calreticulin regions important for structural stability. Biochim Biophys Acta Proteins Proteom. 2021;1869(11):140710. doi:10.1016/j.bbapap.2021.140710
Boelt SG, Norn C, Rasmussen MI, et al. Mapping the Ca2+ induced structural change in calreticulin. J Proteomics. 2016;142:138-148. doi:10.1016/j.jprot.2016.05.015
Schrag JD, Bergeron JJ, Li Y, et al. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell. 2001;8(3):633-644.
Baksh S, Spamer C, Oikawa K, et al. Zn2+ binding to cardiac calsequestrin. Biochem Biophys Res Commun. 1995;209(1):310-315. doi:10.1006/bbrc.1995.1504
Kapoor M, Ellgaard L, Gopalakrishnapai J, et al. Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry. 2004;43(1):97-106.
Clare DK, Saibil HR. ATP-driven molecular chaperone machines. Biopolymers. 2013;99(11):846-859. doi:10.1002/bip.22361
Sucec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client proteins? Front Mol Biosci. 2021;8:762005. doi:10.3389/fmolb.2021.762005
Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J. 1999;18:6718-6729.
Corbett EF, Michalak KM, Oikawa K, et al. The conformation of calreticulin is influenced by the endoplasmic reticulum lumenal environment. J Biol Chem. 2000;275:27177-27185.
Wijeyesakere SJ, Gagnon JK, Arora K, Brooks CL III, Raghavan M. Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP. Proc Natl Acad Sci U S A. 2015;112(41):E5608-E5617. doi:10.1073/pnas.1510132112
Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell. 1999;4:331-341.
Brockmeier A, Williams DB. Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum. Biochemistry. 2006;45(42):12906-12916. doi:10.1021/bi0614378
Elliott JG, Oliver JD, High S. The thiol-dependent reductase ERp57 interacts specifically with N- glycosylated integral membrane proteins. J Biol Chem. 1997;272:13849-13855.
Oliver JD, van der Wal FJ, Bulleid NJ, High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science. 1997;275:86-88.
Kozlov G, Munoz-Escobar J, Castro K, Gehring K. Mapping the ER Interactome: the P domains of Calnexin and Calreticulin as Plurivalent adapters for Foldases and chaperones. Structure. 2017;25(9):1415-1422.e3. doi:10.1016/j.str.2017.07.010
Kozlov G, Bastos-Aristizabal S, Maattanen P, et al. Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J Biol Chem. 2010;285(46):35551-35557.
Ishikawa Y, Vranka JA, Boudko SP, et al. Mutation in cyclophilin B that causes hyperelastosis cutis in American quarter horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding. J Biol Chem. 2012;287(26):22253-22265. doi:10.1074/jbc.M111.333336
Andrin C, Pinkoski MJ, Burns K, et al. Interaction between a Ca2+-binding protein calreticulin and perforin, a component of the cytotoxic T-cell granules. Biochemistry. 1998;37:10386-10394.
Fraser SA, Michalak M, Welch WH, Hudig D. Calreticulin, a component of the endoplasmic reticulum and of cytotoxic lymphocyte granules, regulates perforin-mediated lysis in the hemolytic model system. Biochem Cell Biol. 1998;76:881-887.
Fraser SA, Karimi R, Michalak M, Hudig D. Perforin lytic activity is controlled by calreticulin. J Immunol. 2000;164(8):4150-4155. doi:10.4049/jimmunol.164.8.4150
Nakamura K, Zuppini A, Arnaudeau S, et al. Functional specialization of calreticulin domains. J Cell Biol. 2001;154(5):961-972. doi:10.1083/jcb.200102073
Baksh S, Michalak M. Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains. J Biol Chem. 1991;266:21458-21465.
Mesaeli N, Nakamura K, Zvaritch E, et al. Calreticulin is essential for cardiac development. J Cell Biol. 1999;144:857-868.
Klampfl T, Gisslinger H, Harutyunyan AS, et al. Somatic mutations of calreticulin in myeloproliferative neoplasms. New Engl J Med. 2013;369(25):2379-2390. doi:10.1056/NEJMoa1311347
Nangalia J, Massie CE, Baxter EJ, et al. Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2. New Engl J Med. 2013;369(25):2391-2405. doi:10.1056/NEJMoa1312542
Li J, Prins D, Park HJ, et al. Mutant calreticulin knockin mice develop thrombocytosis and myelofibrosis without a stem cell self-renewal advantage. Blood. 2018;131(6):649-661. doi:10.1182/blood-2017-09-806356
Bergeron JJ, Brenner MB, Thomas DY, Williams DB. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem Sci. 1994;19(3):124-128.
Michalak M, Corbett EF, Mesaeli N, Nakamura K, Opas M. Calreticulin: one protein, one gene, many functions. Biochem J. 1999;344:281-292.
Villamil Giraldo AM, Lopez Medus M, Gonzalez Lebrero M, et al. The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration. J Biol Chem. 2010;285(7):4544-4553. doi:10.1074/jbc.M109.034512
Migliaccio AR, Uversky VN. Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum. J Biomol Struct Dyn. 2018;36(6):1617-1636. doi:10.1080/07391102.2017.1330224
Papadopoulos N, Nedelec A, Derenne A, et al. Oncogenic CALR mutant C-terminus mediates dual binding to the thrombopoietin receptor triggering complex dimerization and activation. Nat Commun. 2023;14(1):1881. doi:10.1038/s41467-023-37277-3
Corbett EF, Michalak KM, Oikawa K, et al. The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment. J Biol Chem. 2000;275(35):27177-27185. doi:10.1074/jbc.M002049200
Baksh S, Spamer C, Heilmann C, Michalak M. Identification of the Zn2+ binding region in calreticulin. FEBS Lett. 1995;376:53-57.
Li Z, Stafford WF, Bouvier M. The metal ion binding properties of calreticulin modulate its conformational flexibility and thermal stability. Biochemistry. 2001;40:11193-11201.
Tan Y, Chen M, Li Z, Mabuchi K, Bouvier M. The calcium- and zinc-responsive regions of calreticulin reside strictly in the N-/C-domain. Biochim Biophys Acta. 2006;1760(5):745-753.
Brecker M, Khakhina S, Schubert TJ, Thompson Z, Rubenstein RC. The probable, possible, and novel functions of ERp29. Front Physiol. 2020;11:574339. doi:10.3389/fphys.2020.574339
Viviano J, Brecker M, Ferrara-Cook C, Suaud L, Rubenstein RC. ERp29 as a regulator of insulin biosynthesis. PLoS One. 2020;15(5):e0233502. doi:10.1371/journal.pone.0233502
Terajima M, Taga Y, Cabral WA, et al. Cyclophilin B deficiency causes abnormal dentin collagen matrix. J Proteome Res. 2017;16(8):2914-2923. doi:10.1021/acs.jproteome.7b00190
Baksh S, Burns K, Andrin C, Michalak M. Interaction of calreticulin with protein disulfide isomerase. J Biol Chem. 1995;270:31338-31344.
Avezov E, Konno T, Zyryanova A, et al. Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum. BMC Biol. 2015;13:2. doi:10.1186/s12915-014-0112-2
Pietra D, Rumi E, Ferretti VV, et al. Differential clinical effects of different mutation subtypes in CALR-mutant myeloproliferative neoplasms. Leukemia. 2016;30(2):431-438. doi:10.1038/leu.2015.277
Prins D, Gonzalez Arias C, Klampfl T, Grinfeld J, Green AR. Mutant Calreticulin in the myeloproliferative neoplasms. Hema. 2020;4(1):e333. doi:10.1097/HS9.0000000000000333
Balligand T, Achouri Y, Pecquet C, et al. Knock-in of murine Calr del52 induces essential thrombocythemia with slow-rising dominance in mice and reveals key role of Calr exon 9 in cardiac development. Leukemia. 2020;34(2):510-521. doi:10.1038/s41375-019-0538-1
Chachoua I, Pecquet C, El-Khoury M, et al. Thrombopoietin receptor activation by myeloproliferative neoplasm associated calreticulin mutants. Blood. 2016;127(10):1325-1335. doi:10.1182/blood-2015-11-681932
Edahiro Y, Araki M, Komatsu N. Mechanism underlying the development of myeloproliferative neoplasms through mutant calreticulin. Cancer Sci. 2020;111(8):2682-2688. doi:10.1111/cas.14503
Masubuchi N, Araki M, Yang Y, et al. Mutant calreticulin interacts with MPL in the secretion pathway for activation on the cell surface. Leukemia. 2020;34(2):499-509. doi:10.1038/s41375-019-0564-z
Pecquet C, Chachoua I, Roy A, et al. Calreticulin mutants as oncogenic rogue chaperones for TpoR and traffic-defective pathogenic TpoR mutants. Blood. 2019;133(25):2669-2681. doi:10.1182/blood-2018-09-874578
Shide K, Kameda T, Kamiunten A, et al. Calreticulin haploinsufficiency augments stem cell activity and is required for onset of myeloproliferative neoplasms in mice. Blood. 2020;136(1):106-118. doi:10.1182/blood.2019003358
Venkatesan A, Geng J, Kandarpa M, et al. Mechanism of mutant calreticulin-mediated activation of the thrombopoietin receptor in cancers. J Cell Biol. 2021;220(7):e202009179. doi:10.1083/jcb.202009179
Guijarro-Hernandez A, Vizmanos JL. A broad overview of signaling in Ph-negative classic myeloproliferative neoplasms. Cancer. 2021;13(5):984. doi:10.3390/cancers13050984
Pecquet C, Papadopoulos N, Balligand T, et al. Secreted mutant Calreticulins As rogue cytokines in myeloproliferative neoplasms. Blood. 2022;141(8):917-929. doi:10.1182/blood.2022016846
Liu P, Zhao L, Loos F, et al. Immunosuppression by mutated Calreticulin released from malignant cells. Mol Cell. 2020;77(4):748-760. doi:10.1016/j.molcel.2019.11.004
Ibarra J, Elbanna YA, Kurylowicz K, et al. Type I but not type II Calreticulin mutations activate the IRE1alpha/XBP1 pathway of the unfolded protein response to drive myeloproliferative neoplasms. Blood Cancer Discov. 2022;3(4):298-315. doi:10.1158/2643-3230.BCD-21-0144
Bayes de Luna A, Elosua R. Sudden death. Rev Esp Cardiol. 2012;65(11):1039-1052. doi:10.1016/j.recesp.2012.03.032
Kuriachan VP, Sumner GL, Mitchell LB. Sudden cardiac death. Curr Probl Cardiol. 2015;40(4):133-200. doi:10.1016/j.cpcardiol.2015.01.002
Kumar A, Avishay DM, Jones CR, et al. Sudden cardiac death: epidemiology, pathogenesis and management. Rev Cardiovasc Med. 2021;22(1):147-158. doi:10.31083/j.rcm.2021.01.207
Michalak M, Agellon LB. Stress coping strategies in the heart: an integrated view. Front Cardiovas Med. 2018;5:168. doi:10.3389/fcvm.2018.00168
Agellon LB, Michalak M. The endoplasmic reticulum and the cellular reticular network. Adv Exp Med Biol. 2017;981:61-76. doi:10.1007/978-3-319-55858-5_4
Voeltz GK, Barr FA. Cell organelles. Curr Opin Cell Biol. 2013;25(4):403-405. doi:10.1016/j.ceb.2013.06.001
Chen X, Cubillos-Ruiz JR. Endoplasmic reticulum stress signals in the tumour and its microenvironment. Nat Rev Cancer. 2021;21(2):71-88. doi:10.1038/s41568-020-00312-2
English AR, Voeltz GK. Endoplasmic reticulum structure and interconnections with other organelles. Cold Spring Harb Perspect Biol. 2013;5(4):a013227. doi:10.1101/cshperspect.a013227
Almeida C, Amaral MD. A central role of the endoplasmic reticulum in the cell emerges from its functional contact sites with multiple organelles. Cell Mol Life Sci. 2020;77(23):4729-4745. doi:10.1007/s00018-020-03523-w
Huang Y, Ji J, Zhao Q, Song J. Editorial: regulation of endoplasmic reticulum and mitochondria in cellular homeostasis. Front Cell Dev Biol. 2022;10:1004376. doi:10.3389/fcell.2022.1004376
Mesgarzadeh JS, Buxbaum JN, Wiseman RL. Stress-responsive regulation of extracellular proteostasis. J Cell Biol. 2022;221(4):e202112104. doi:10.1083/jcb.202112104
Sassano ML, Felipe-Abrio B, Agostinis P. ER-mitochondria contact sites; a multifaceted factory for Ca2+ signaling and lipid transport. Front Cell Dev Biol. 2022;10:988014. doi:10.3389/fcell.2022.988014
Wang WA, Agellon LB, Michalak M. Endoplasmic reticulum calcium dictates the distribution of intracellular unesterified cholesterol. Cell Calcium. 2018;76:116-121. doi:10.1016/j.ceca.2018.11.002
Burdakov D, Ole H, Petersen B, Verkhratsky A. Intraluminal calcium as a primary regulator of endoplasmic reticulum function. Cell Calcium. 2005;38:303-310.
Levine TP, Patel S. Signalling at membrane contact sites: two membranes come together to handle second messengers. Curr Opin Cell Biol. 2016;39:77-83. doi:10.1016/j.ceb.2016.02.011
Phillips MJ, Voeltz GK. Structure and function of ER membrane contact sites with other organelles. Nat Rev Mol Cell Biol. 2016;17(2):69-82. doi:10.1038/nrm.2015.8
Terasaki M, Runft LL, Hand AR. Changes in organization of the endoplasmic reticulum during Xenopus oocyte maturation and activation. Mol Biol Cell. 2001;12(4):1103-1116. doi:10.1091/mbc.12.4.1103
Saavedra MD, Mondejar I, Coy P, et al. Calreticulin from suboolemmal vesicles affects membrane regulation of polyspermy. Reproduction. 2014;147(3):369-378. doi:10.1530/REP-13-0454
Nair S, Wearsch PA, Mitchell DA, Wassenberg JJ, Gilboa E, Nicchitta CV. Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. J Immunol. 1999;162:6426-6432.
Pagny S, Cabanes-Macheteau M, Gillikin JW, et al. Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention. Plant Cell. 2000;12(5):739-756. doi:10.1105/tpc.12.5.739
Ding W, Albrecht B, Luo R, et al. Endoplasmic reticulum and cis-Golgi localization of human T-lymphotropic virus type 1 p12(I): association with calreticulin and calnexin. J Virol. 2001;75(16):7672-7682. doi:10.1128/JVI.75.16.7672-7682.2001
Goicoechea S, Orr AW, Pallero MA, Eggleton P, Murphy-Ullrich JE. Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J Biol Chem. 2000;275(46):36358-36368. doi:10.1074/jbc.M005951200
Goicoechea S, Pallero MA, Eggleton P, Michalak M, Murphy-Ullrich JE. The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin. J Biol Chem. 2002;277(40):37219-37228. doi:10.1074/jbc.M202200200
Orr AW, Pedraza CE, Pallero MA, et al. Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly. J Cell Biol. 2003;161(6):1179-1189. doi:10.1083/jcb.200302069
Pandya UM, Manzanares MA, Tellechea A, et al. Calreticulin exploits TGF-beta for extracellular matrix induction engineering a tissue regenerative process. FASEB J. 2020;34(12):15849-15874. doi:10.1096/fj.202001161R
Nanney LB, Woodrell CD, Greives MR, et al. Calreticulin enhances porcine wound repair by diverse biological effects. Am J Pathol. 2008;173(3):610-630. doi:10.2353/ajpath.2008.071027
Greives MR, Samra F, Pavlides SC, et al. Exogenous calreticulin improves diabetic wound healing. Wound Repair Regen. 2012;20(5):715-730. doi:10.1111/j.1524-475X.2012.00822.x
Gold LI, Rahman M, Blechman KM, et al. Overview of the role for calreticulin in the enhancement of wound healing through multiple biological effects. J Investig Dermatol Symp Proc. 2006;11(1):57-65. doi:10.1038/sj.jidsymp.5650011
Stack ME, Mishra S, Parimala Chelvi Ratnamani M, Wang H, Gold LI, Wang H. Biomimetic extracellular matrix nanofibers electrospun with Calreticulin promote synergistic activity for tissue regeneration. ACS Appl Mater Interfaces. 2022;14(46):51683-51696. doi:10.1021/acsami.2c13887
Cockram TOJ, Puigdellivol M, Brown GC. Calreticulin and Galectin-3 opsonise bacteria for phagocytosis by microglia. Front Immunol 2019;10:2647. 10.3389/fimmu.2019.02647
Reid KM, Kitchener EJA, Butler CA, Cockram TOJ, Brown GC. Brain cells release Calreticulin that attracts and activates microglia, and inhibits amyloid Beta aggregation and neurotoxicity. Front Immunol. 2022;13:859686. doi:10.3389/fimmu.2022.859686
Dai E, Stewart M, Ritchie B, et al. Calreticulin, a potential vascular regulatory protein, reduces intimal hyperplasia after arterial injury. Arterioscler Thromb Vasc Biol. 1997;17:2359-2368.
Gardai SJ, McPhillips KA, Frasch SC, et al. Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell. 2005;123(2):321-334. doi:10.1016/j.cell.2005.08.032
Obeid M, Tesniere A, Ghiringhelli F, et al. Calreticulin exposure dictates the immunogenicity of cancer cell death. Nat Med. 2007;13(1):54-61.
Krysko DV, Garg AD, Kaczmarek A, Krysko O, Agostinis P, Vandenabeele P. Immunogenic cell death and DAMPs in cancer therapy. Nat Rev Cancer. 2012;12(12):860-875. doi:10.1038/nrc3380
Chao MP, Jaiswal S, Weissman-Tsukamoto R, et al. Calreticulin is the dominant pro-phagocytic signal on multiple human cancers and is counterbalanced by CD47. Sci Transl Med. 2010;2(63):63ra94. doi:10.1126/scitranslmed.3001375
Garg AD, Krysko DV, Verfaillie T, et al. A novel pathway combining calreticulin exposure and ATP secretion in immunogenic cancer cell death. EMBO J. 2012;31(5):1062-1079. doi:10.1038/emboj.2011.497
Kliueva NG, Roskin GI. The antibiotic cruzin and its mechanism of action on cancer cells. Izv Akad Nauk Kirg Ssr Biol. 1963;3:366-390.
Ferreira V, Molina MC, Valck C, et al. Role of calreticulin from parasites in its interaction with vertebrate hosts. Mol Immunol. 2004;40(17):1279-1291. doi:10.1016/j.molimm.2003.11.018
Ferreira V, Valck C, Sanchez G, et al. The classical activation pathway of the human complement system is specifically inhibited by calreticulin from Trypanosoma cruzi. J Immunol. 2004;172(5):3042-3050. doi:10.4049/jimmunol.172.5.3042
Lopez NC, Valck C, Ramirez G, et al. Antiangiogenic and antitumor effects of Trypanosoma cruzi Calreticulin. PLoS Negl Trop Dis. 2010;4(7):e730. doi:10.1371/journal.pntd.0000730
Cruz P, Sosoniuk-Roche E, Maldonado I, Torres CG, Ferreira A. Trypanosoma cruzi calreticulin: In vitro modulation of key immunogenic markers of both canine tumors and relevant immune competent cells. Immunobiology. 2020;225(2):151892. doi:10.1016/j.imbio.2019.12.001
Pena Alvarez J, Teneb J, Maldonado I, et al. Structural bases that underline Trypanosoma cruzi calreticulin proinfective, antiangiogenic and antitumor properties. Immunobiology. 2020;225(1):151863. doi:10.1016/j.imbio.2019.10.012
Ramirez-Toloza G, Sosoniuk-Roche E, Valck C, Aguilar-Guzman L, Ferreira VP, Ferreira A. Trypanosoma cruzi Calreticulin: immune evasion, infectivity, and tumorigenesis. Trends Parasitol. 2020;36(4):368-381. doi:10.1016/j.pt.2020.01.007
Sosoniuk-Roche E, Cruz P, Maldonado I, et al. In vitro treatment of a murine mammary adenocarcinoma cell line with recombinant Trypanosoma cruzi Calreticulin promotes immunogenicity and phagocytosis. Mol Immunol. 2020;124:51-60. doi:10.1016/j.molimm.2020.05.013
Ramirez-Toloza G, Aguilar-Guzman L, Valck C, Ferreira VP, Ferreira A. The interactions of parasite Calreticulin with initial complement components: consequences in immunity and virulence. Front Immunol. 2020;11:1561. doi:10.3389/fimmu.2020.01561
Panaretakis T, Joza N, Modjtahedi N, et al. The co-translocation of ERp57 and calreticulin determines the immunogenicity of cell death. Cell Death Differ. 2008;15:1499-1509.
Wiersma VR, Michalak M, Abdullah TM, Bremer E, Eggleton P. Mechanisms of translocation of ER chaperones to the cell surface and immunomodulatory roles in cancer and autoimmunity. Front Oncol. 2015;5:7. doi:10.3389/fonc.2015.00007
Benyair R, Ron E, Lederkremer GZ. Protein quality control, retention, and degradation at the endoplasmic reticulum. Int Rev Cell Mol Biol. 2011;292:197-280. doi:10.1016/B978-0-12-386033-0.00005-0
Wearsch PA, Cresswell P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol. 2008;20(6):624-631. doi:10.1016/j.ceb.2008.09.005
Blum JS, Wearsch PA, Cresswell P. Pathways of antigen processing. Annu Rev Immunol. 2013;31:443-473. doi:10.1146/annurev-immunol-032712-095910
Sun Z, Brodsky JL. Protein quality control in the secretory pathway. J Cell Biol. 2019;218(10):3171-3187. doi:10.1083/jcb.201906047
Hol EM, Scheper W. Protein quality control in neurodegeneration: walking the tight rope between health and disease. J Mol Neurosci. 2008;34(1):23-33. doi:10.1007/s12031-007-0013-8
Dejgaard S, Nicolay J, Taheri M, Thomas DY, Bergeron JJ. The ER glycoprotein quality control system. Curr Issues Mol Biol. 2004;6(1):29-42.
Koerner CM, Roberts BS, Neher SB. Endoplasmic reticulum quality control in lipoprotein metabolism. Mol Cell Endocrinol. 2019;498:110547. doi:10.1016/j.mce.2019.110547
Chino H, Mizushima N. ER-Phagy: Quality and quantity control of the endoplasmic reticulum by autophagy. Cold Spring Harb Perspect Biol. 2022;15(1):a041256. 10.1101/cshperspect.a041256
Molinari M, Hebert DN. Glycoprotein maturation and quality control. Semin Cell Dev Biol. 2015;41:70. doi:10.1016/j.semcdb.2015.05.009
Lamriben L, Graham JB, Adams BM, Hebert DN. N-glycan-based ER molecular chaperone and protein quality control system: the Calnexin binding cycle. Traffic. 2016;17(4):308-326. doi:10.1111/tra.12358
Danilczyk UG, Cohen-Doyle MF, Williams DB. Functional relationship between Calreticulin, Calnexin, and the endoplasmic reticulum luminal domain of Calnexin. J Biol Chem. 2000;275(17):13089-13097.
Kang SJ, Cresswell P. Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain. J Biol Chem. 2002;277(47):44838-44844. doi:10.1074/jbc.M207831200
Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity. 1996;5(2):103-114.
Gao B, Adhikari R, Howarth M, et al. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity. 2002;16(1):99-109.
Chapman DC, Williams DB. ER quality control in the biogenesis of MHC class I molecules. Semin Cell Dev Biol. 2010;21(5):512-519. doi:10.1016/j.semcdb.2009.12.013
Margulies DH, Taylor DK, Jiang J, et al. Chaperones and catalysts: How antigen presentation pathways cope with biological necessity. Front Immunol. 2022;13:859782. doi:10.3389/fimmu.2022.859782
Arshad N, Cresswell P. Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I. J Biol Chem. 2018;293(25):9555-9569. doi:10.1074/jbc.RA118.002836
Arshad N, Cresswell P. Impact of Calreticulin and its mutants on endoplasmic reticulum function in health and disease. Prog Mol Subcell Biol. 2021;59:163-180. doi:10.1007/978-3-030-67696-4_8
Peaper DR, Cresswell P. Regulation of MHC class I assembly and peptide binding. Annu Rev Cell Dev Biol. 2008;24:343-368.
Corbett EF, Michalak M. Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem Sci. 2000;25(7):307-311.
Yu R, Hinkle PM. Rapid turnover of calcium in the endoplasmic reticulum during signaling. Studies with cameleon calcium indicators. J Biol Chem. 2000;275(31):23648-23653.
Solovyova N, Fernyhough P, Glazner G, Verkhratsky A. Xestospongin C empties the ER calcium store but does not inhibit InsP3-induced Ca2+ release in cultured dorsal root ganglia neurones. Cell Calcium. 2002;32(1):49-52.
Alvarez J, Montero M. Measuring [Ca2+] in the endoplasmic reticulum with aequorin. Cell Calcium. 2002;32(5-6):251-260. doi:10.1016/s0143416002001860
Bygrave FL, Benedetti A. What is the concentration of calcium ions in the endoplasmic reticulum? Cell Calcium. 1996;19(6):547-551. doi:10.1016/s0143-4160(96)90064-0
Rossi AM, Taylor CW. Reliable measurement of free Ca2+ concentrations in the ER lumen using mag-Fluo-4. Cell Calcium. 2020;87:102188. doi:10.1016/j.ceca.2020.102188
Berridge MJ, Lipp P, Bootman MD. The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol. 2000;1(1):11-21.
Petersen OH, Verkhratsky A. Endoplasmic reticulum calcium tunnels integrate signalling in polarised cells. Cell Calcium. 2007;42(4-5):373-378. doi:10.1016/j.ceca.2007.05.012
Holcman D, Parutto P, Chambers JE, et al. Single particle trajectories reveal active endoplasmic reticulum luminal flow. Nat Cell Biol. 2018;20(10):1118-1125. doi:10.1038/s41556-018-0192-2
Corbett EF, Oikawa K, Francois P, et al. Ca2+ regulation of interactions between endoplasmic reticulum chaperones. J Biol Chem. 1999;274(10):6203-6211.
Tanikawa Y, Kanemura S, Ito D, et al. Ca2+ regulates ERp57-Calnexin complex formation. Molecules. 2021;26(10):2853. doi:10.3390/molecules26102853
Santulli G, Nakashima R, Yuan Q, Marks AR. Intracellular calcium release channels: an update. J Physiol. 2017;595(10):3041-3051. doi:10.1113/JP272781
Prole DL, Taylor CW. Structure and function of IP3 receptors. Cold Spring Harb Perspect Biol. 2019;11(4):a035063. 10.1101/cshperspect.a035063
Roos J, DiGregorio PJ, Yeromin AV, et al. STIM1, an essential and conserved component of store-operated Ca2+ channel function. J Cell Biol. 2005;169(3):435-445.
Soboloff J, Rothberg BS, Madesh M, Gill DL. STIM proteins: dynamic calcium signal transducers. Nat Rev Mol Cell Biol. 2012;13(9):549-565. doi:10.1038/nrm3414
Liou J, Kim ML, Heo WD, et al. STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx. Curr Biol. 2005;15(13):1235-1241.
Zhang SL, Yu Y, Roos J, et al. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature. 2005;437(7060):902-905.
Wang WA, Demaurex N. Proteins interacting with STIM1 and store-operated Ca2+ entry. Prog Mol Subcell Biol. 2021;59:51-97. doi:10.1007/978-3-030-67696-4_4
Bodnar D, Chung WY, Yang D, Hong JH, Jha A, Muallem S. STIM-TRP pathways and microdomain organization: Ca2+ influx channels: the Orai-STIM1-TRPC complexes. Adv Exp Med Biol. 2017;993:139-157. doi:10.1007/978-3-319-57732-6_8
Wang X, Deng Y, Zhang G, et al. Spliced x-box binding protein 1 stimulates adaptive growth through activation of mTOR. Circulation. 2019;140(7):566-579. doi:10.1161/circulationaha.118.038924
Coe H, Michalak M. Calcium binding chaperones of the endoplasmic reticulum. Gen Physiol Biophys. 2009;28:F96-F103.
Serwach K, Gruszczynska-Biegala J. Target molecules of STIM proteins in the central nervous system. Front Mol Neurosci. 2020;13:617422. doi:10.3389/fnmol.2020.617422
Camacho P, Lechleiter JD. Calreticulin inhibits repetitive intracellular Ca2+ waves. Cell. 1995;82(5):765-771.
John LM, Lechleiter JD, Camacho P. Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol. 1998;142:963-973.
Li Y, Camacho P. Ca2+-dependent redox modulation of SERCA2b by ERp57. J Cell Biol. 2004;164(1):35-46.
Xu W, Longo FJ, Wintermantel MR, Jiang X, Clark RA, DeLisle S. Calreticulin modulates capacitative Ca2+ influx by controlling the extent of inositol 1,4,5-trisphosphate-induced Ca2+ store depletion. J Biol Chem. 2000;275(47):36676-36682. doi:10.1074/jbc.M002041200
Arnaudeau S, Frieden M, Nakamura K, Castelbou C, Michalak M, Demaurex N. Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J Biol Chem. 2002;277(48):46696-46705. doi:10.1074/jbc.M202395200
Di Buduo CA, Abbonante V, Marty C, et al. Defective interaction of mutant calreticulin and SOCE in megakaryocytes from patients with myeloproliferative neoplasms. Blood. 2020;135(2):133-144. doi:10.1182/blood.2019001103
Prins D, Groenendyk J, Touret N, Michalak M. Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57. EMBO rep. 2011;12(11):1182-1188. doi:10.1038/embor.2011.173
Papp S, Dziak E, Michalak M, Opas M. Is all of the endoplasmic reticulum created equal? The effects of the heterogeneous distribution of endoplasmic reticulum Ca2+-handling proteins. J Cell Biol. 2003;160(4):475-479.
Nguyen DT, Le TM, Hattori T, et al. The ATF6beta-calreticulin axis promotes neuronal survival under endoplasmic reticulum stress and excitotoxicity. Sci rep. 2021;11(1):13086. doi:10.1038/s41598-021-92529-w
Tanaka T, Nguyen DT, Kwankaew N, et al. ATF6beta deficiency elicits anxiety-like behavior and hyperactivity under stress conditions. Neurochem Res. 2023;48(7):2175-2186. doi:10.1007/s11064-023-03900-4
Bravo R, Vicencio JM, Parra V, et al. Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress. J Cell Sci. 2011;124(13):2143-2152. doi:10.1242/jcs.080762
Yong J, Bischof H, Burgstaller S, et al. Mitochondria supply ATP to the ER through a mechanism antagonized by cytosolic Ca2+. Elife. 2019;8:49682. doi:10.7554/eLife.49682
Wang Q, Calsequestrin MM. Structure, function, and evolution. Cell Calcium. 2020;90:102242. doi:10.1016/j.ceca.2020.102242
Rossi D, Gamberucci A, Pierantozzi E, Amato C, Migliore L, Sorrentino V. Calsequestrin, a key protein in striated muscle health and disease. J Muscle Res Cell Motil. 2021;42(2):267-279. doi:10.1007/s10974-020-09583-6
Galligan JJ, Petersen DR. The human protein disulfide isomerase gene family. Hum Genomics. 2012;6:6. doi:10.1186/1479-7364-6-6
Kim E, Youn B, Kemper L, et al. Characterization of human cardiac calsequestrin and its deleterious mutants. J Mol Biol. 2007;373(4):1047-1057. doi:10.1016/j.jmb.2007.08.055
Gatti G, Trifari S, Mesaeli M, Parker JMR, Michalak M, Meldolesi J. Head-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of ER luminal proteins. J Cell Biol. 2001;154:525-534.
Kumar A, Chakravarty H, Bal NC, et al. Identification of calcium binding sites on calsequestrin 1 and their implications for polymerization. Mol Biosyst. 2013;9(7):1949-1957. doi:10.1039/c3mb25588c
Rauch F, Prud'homme J, Arabian A, Dedhar S, St-Arnaud R. Heart, brain, and body wall defects in mice lacking calreticulin. Exp Cell Res. 2000;256:105-111.
Li J, Puceat M, Perez-Terzic C, et al. Calreticulin reveals a critical Ca2+ checkpoint in cardiac myofibrillogenesis. J Cell Biol. 2002;158(1):103-113.
Dewenter M, von der Lieth A, Katus HA, Backs J. Calcium signaling and transcriptional regulation in Cardiomyocytes. Circ Res. 2017;121(8):1000-1020. doi:10.1161/CIRCRESAHA.117.310355
Porter GA Jr, Makuck RF, Rivkees SA. Intracellular calcium plays an essential role in cardiac development. Dev Dyn. 2003;227(2):280-290. doi:10.1002/dvdy.10307
Guo L, Nakamura K, Lynch J, et al. Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse. J Biol Chem. 2002;277(52):50776-50779.
Molkentin JD. Calcineurin and beyond: cardiac hypertrophic signaling. Circ Res. 2000;87(9):731-738. doi:10.1161/01.res.87.9.731
Tyser RC, Miranda AM, Chen CM, Davidson SM, Srinivas S, Riley PR. Calcium handling precedes cardiac differentiation to initiate the first heartbeat. Elife. 2016;5:17113. doi:10.7554/Elife.17113
Lynch JM, Chilibeck K, Qui Y, Michalak M. Assembling pieces of the cardiac puzzle; calreticulin and calcium-dependent pathways in cardiac development, health, and disease. Trends Cardiovasc Med. 2006;16(3):65-69.
Molkentin JD, Lu JR, Antos CL, et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell. 1998;93:215-228.
Crabtree GR, Olson EN. NFAT signaling: choreographing the social lives of cells. Cell. 2002;109:S67-S79.
O'Keefe SJ, Tamura J, Kincaid RL, Tocci MJ, O'Neill EA. FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature. 1992;357:692-694.
Jaconi M, Bony C, Richards SM, et al. Inositol 1,4,5-trisphosphate directs Ca2+ flow between mitochondria and the endoplasmic/sarcoplasmic reticulum: a role in regulating cardiac autonomic Ca2+ spiking. Mol Biol Cell. 2000;11(5):1845-1858.
Mery A, Aimond F, Menard C, Mikoshiba K, Michalak M, Puceat M. Initiation of embryonic cardiac pacemaker activity by inositol 1,4,5-trisphosphate-dependent calcium signaling. Mol Biol Cell. 2005;16(5):2414-2423.
Michalak M, Burns K, Andrin C, et al. Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression. J Biol Chem. 1996;271:29436-29445.
Shago M, Flock G, Leung Hagesteijn CY, et al. Modulation of the retinoic acid and retinoid X receptor signaling pathways in P19 embryonal carcinoma cells by calreticulin. Exp Cell Res. 1997;230:50-60.
Dedhar S, Rennie PS, Shago M, et al. Inhibition of nuclear hormone receptor activity by calreticulin. Nature. 1994;367:480-483.
Burns K, Duggan B, Atkinson EA, et al. Modulation of gene expression by calreticulin binding to the glucocorticoid receptor. Nature. 1994;367:476-480.
Burns K, Opas M, Michalak M. Calreticulin inhibits glucocorticoid- but not cAMP-sensitive expression of tyrosine aminotransferase gene in cultured McA-RH7777 hepatocytes. Mol Cell Biochem. 1997;171:37-43.
Nakamura K, Robertson M, Liu G, et al. Complete heart block and sudden death in mice overexpressing calreticulin. J Clin Invest. 2001;107(10):1245-1253.
Baruteau AE, Pass RH, Thambo JB, et al. Congenital and childhood atrioventricular blocks: pathophysiology and contemporary management. Eur J Pediatr. 2016;175(9):1235-1248. doi:10.1007/s00431-016-2748-0
Lee D, Oka T, Hunter B, et al. Calreticulin induces dilated cardiomyopathy. PLoS One. 2013;8(2):e56387. doi:10.1371/journal.pone.0056387
Groenendyk J, Lee D, Jung J, et al. Inhibition of the unfolded protein response mechanism prevents cardiac fibrosis. PLoS One. 2016;11(7):e0159682. doi:10.1371/journal.pone.0159682
Beuers U, Nathanson MH, Boyer JL. Effects of tauroursodeoxycholic acid on cytosolic Ca2+ signals in isolated rat hepatocytes. Gastroenterology. 1993;104(2):604-612. doi:10.1016/0016-5085(93)90433-d
Turdi S, Hu N, Ren J. Tauroursodeoxycholic acid mitigates high fat diet-induced cardiomyocyte contractile and intracellular Ca2+ anomalies. PLoS One. 2013;8(5):e63615. doi:10.1371/journal.pone.0063615
Lebeau PF, Platko K, Byun JH, Austin RC. Calcium as a reliable marker for the quantitative assessment of endoplasmic reticulum stress in live cells. J Biol Chem. 2021;296:100779. doi:10.1016/j.jbc.2021.100779
Knollmann BC, Chopra N, Hlaing T, et al. Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia. J Clin Invest. 2006;116(9):2510-2520. doi:10.1172/JCI29128
Song L, Alcalai R, Arad M, et al. Calsequestrin 2 (CASQ2) mutations increase expression of calreticulin and ryanodine receptors, causing catecholaminergic polymorphic ventricular tachycardia. J Clin Invest. 2007;117(7):1814-1823. doi:10.1172/JCI31080