Erratum: Prion Protein Misfolding Affects Calcium Homeostasis and Sensitizes Cells to Endoplasmic Reticulum Stress (PLoS ONE (2021) 5:12 (e15658) DOI: 10.1371/journal.pone.0015658);Prion Protein Misfolding Affects Calcium Homeostasis and Sensitizes Cells to Endoplasmic Reticulum Stress

PLoS ONE

Volumn 5, Issue 12, 2010, Pages

  Torres, Mauricio ^a   Castillo, Karen ^a   Armisén, Ricardo ^a   Stutzin, Andrés ^a   Soto, Claudio ^b   Hetz, Claudio ^a,c,d  

^a UNIVERSITY OF CHILE   (Chile)

^b UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^c Neurounion Biomedical Foundation   (Chile)

^d HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; CALCIUM; CHAPERONE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; CALCIUM CELL LEVEL; CALCIUM HOMEOSTASIS; CALCIUM TRANSPORT; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; MOUSE; NEUROPATHOLOGY; NEUROTOXICITY; NONHUMAN; PRION; PRION DISEASE; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; VIRUS REPLICATION; ANIMAL; CELL MEMBRANE; CHEMISTRY; CREUTZFELDT JAKOB DISEASE; ENDOPLASMIC RETICULUM; HOMEOSTASIS; HUMAN; METABOLISM; PROTEIN DENATURATION; SCRAPIE; UPREGULATION;

ANIMALS; CALCIUM; CELL MEMBRANE; CREUTZFELDT-JAKOB SYNDROME; ENDOPLASMIC RETICULUM; HOMEOSTASIS; HUMANS; MICE; MOLECULAR CHAPERONES; PRIONS; PROTEIN DENATURATION; PROTEIN FOLDING; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; SCRAPIE; UP-REGULATION;

EID: 78650843400     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0262628     Document Type: Erratum

References (66)

1. Matus S, Lisbona F, Torres M, Leon C, Thielen P, et al. (2008) The stress rheostat: an interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration. Curr Mol Med 8: 157-172.
2. Prusiner SB (1998) Prions. Proc Natl Acad Sci U S A 95: 13363-13383.
3. Hetz C, Soto C (2003) Protein misfolding and disease: the case of prion disorders. Cell Mol Life Sci 60: 133-143.
4. Soto C, Saborio GP (2001) Prions: disease propagation and disease therapy by conformational transmission. Trends Mol Med 7: 109-114.
5. Hegde RS, Rane NS (2003) Prion protein trafficking and the development of neurodegeneration. Trends Neurosci 26: 337-339.
6. Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A (2001) Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. Embo J 20: 5383-5391.
7. Jin T, Gu Y, Zanusso G, Sy M, Kumar A, et al. (2000) The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J Biol Chem 275: 38699-38704.
8. Ma J, Lindquist S (2001) Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci U S A 98: 14955-14960.
9. Stewart RS, Drisaldi B, Harris DA (2001) A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum. Mol Biol Cell 12: 881-889.
10. Gu Y, Verghese S, Bose S, Mohan M, Singh N (2007) Mutant prion protein D202N associated with familial prion disease is retained in the endoplasmic reticulum and forms 'curly' intracellular aggregates. J Mol Neurosci 32: 90-96.
11. Zanusso G, Petersen RB, Jin T, Jing Y, Kanoush R, et al. (1999) Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein. J Biol Chem 274: 23396-23404.
12. Hetz CA, Soto C (2006) Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr Mol Med 6: 37-43.
13. Drisaldi B, Stewart RS, Adles C, Stewart LR, Quaglio E, et al. (2003) Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J Biol Chem 278: 21732-21743.
14. Singh N, Zanusso G, Chen SG, Fujioka H, Richardson S, et al. (1997) Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation. J Biol Chem 272: 28461-28470.
15. Ivanova L, Barmada S, Kummer T, Harris DA (2001) Mutant prion proteins are partially retained in the endoplasmic reticulum. J Biol Chem 276: 42409-42421.
16. Stewart RS, Piccardo P, Ghetti B, Harris DA (2005) Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein. J Neurosci 25: 3469-3477.
17. Stewart RS, Harris DA (2005) A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons. J Biol Chem 280: 15855-15864.
18. Vey M, Pilkuhn S, Wille H, Nixon R, DeArmond SJ, et al. (1996) Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci U S A 93: 14945-14949.
19. Naslavsky N, Stein R, Yanai A, Friedlander G, Taraboulos A (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J Biol Chem 272: 6324-6331.
20. Marella M, Lehmann S, Grassi J, Chabry J (2002) Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release. J Biol Chem 277: 25457-25464.
21. Beranger F, Mange A, Goud B, Lehmann S (2002) Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J Biol Chem 277: 38972-38977.
22. Rane NS, Kang SW, Chakrabarti O, Feigenbaum L, Hegde RS (2008) Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Dev Cell 15: 359-370.
23. Taraboulos A, Serban D, Prusiner SB (1990) Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J Cell Biol 110: 2117-2132.
24. Kristiansen M, Deriziotis P, Dimcheff DE, Jackson GS, Ovaa H, et al. (2007) Disease-associated prion protein oligomers inhibit the 26S proteasome. Mol Cell 26: 175-188.
25. Grenier C, Bissonnette C, Volkov L, Roucou X (2006) Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and nonneuronal cells. J Neurochem 97: 1456-1466.
26. Kristiansen M, Messenger MJ, Klohn PC, Brandner S, Wadsworth JD, et al. (2005) Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis. J Biol Chem 280: 38851-38861.
27. Ma J, Lindquist S (2002) Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298: 1785-1788.
28. Hetz C, Glimcher LH (2009) Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome. Mol Cell 35: 551-561.
29. Hetz CA (2007) ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage. Antioxid Redox Signal 9: 2345-2355.
30. Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C (2003) Caspase- 12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. Embo J 22: 5435-5445.
31. Yoo BC, Krapfenbauer K, Cairns N, Belay G, Bajo M, et al. (2002) Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease. Neurosci Lett 334: 196-200.
32. Brown AR, Rebus S, McKimmie CS, Robertson K, Williams A, et al. (2005) Gene expression profiling of the preclinical scrapie-infected hippocampus. Biochem Biophys Res Commun 334: 86-95.
33. Hetz C, Lee AH, Gonzalez-Romero D, Thielen P, Castilla J, et al. (2008) Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc Natl Acad Sci U S A 105: 757-762.
34. Hetz C, Russelakis-Carneiro M, Walchli S, Carboni S, Vial-Knecht E, et al. (2005) The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity. J Neurosci 25: 2793-2802.
35. Steele AD, Hetz C, Yi CH, Jackson WS, Borkowski AW, et al. (2007) Prion pathogenesis is independent of caspase-12. Prion 1: 243-247.
36. Xu K, Wang X, Shi Q, Chen C, Tian C, et al. Human Prion Protein Mutants with Deleted and Inserted Octarepeats Undergo Different Pathways to Trigger Cell Apoptosis. J Mol Neurosci.
37. Orsi A, Fioriti L, Chiesa R, Sitia R (2006) Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J Biol Chem 281: 30431-30438.
38. Apodaca J, Kim I, Rao H (2006) Cellular tolerance of prion protein PrP in yeast involves proteolysis and the unfolded protein response. Biochem Biophys Res Commun 347: 319-326.
39. Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CM (2006) An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol Dis 23: 669-678.
40. Ferreiro E, Costa R, Marques S, Cardoso SM, Oliveira CR, et al. (2008) Involvement of mitochondria in endoplasmic reticulum stress-induced apoptotic cell death pathway triggered by the prion peptide PrP(106-126). J Neurochem 104: 766-776.
41. Gorlach A, Klappa P, Kietzmann T (2006) The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Signal 8: 1391-1418.
42. Puzianowska-Kuznicka M, Kuznicki J (2009) The ER and ageing II: calcium homeostasis. Ageing Res Rev 8: 160-172.
43. 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32: 269-278.
44. 2+ increases enhance mutant glucocerebrosidase proteostasis. Nat Chem Biol 6: 424-432.
45. 2+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity. Proc Natl Acad Sci U S A.
46. Agostinho P, Oliveira CR (2003) Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides. Eur J Neurosci 17: 1189-1196.
47. Florio T, Grimaldi M, Scorziello A, Salmona M, Bugiani O, et al. (1996) Intracellular calcium rise through L-type calcium channels, as molecular mechanism for prion protein fragment 106-126-induced astroglial proliferation. Biochem Biophys Res Commun 228: 397-405.
48. Kawahara M, Kuroda Y, Arispe N, Rojas E (2000) Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J Biol Chem 275: 14077-14083.
49. O'Donovan CN, Tobin D, Cotter TG (2001) Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SHSY5Y cells. J Biol Chem 276: 43516-43523.
50. Thellung S, Florio T, Villa V, Corsaro A, Arena S, et al. (2000) Apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in rat cerebellar granule cells treated with the prion protein fragment 106-126. Neurobiol Dis 7: 299-309.
51. Ferreiro E, Oliveira CR, Pereira CM (2008) The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol Dis 30: 331-342.
52. Nakagawa T, Zhu H, Morishima N, Li E, Xu J, et al. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloidbeta. Nature 403: 98-103.
53. 2+: a control point for apoptosis. Science 300: 135-139.
54. 2+ homeostasis downstream of Bcl-2 family proteins. J Biol Chem 283: 11477-11484.
55. Berridge MJ (2002) The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32: 235-249.
56. Harris DA (1999) Cellular biology of prion diseases. Clin Microbiol Rev 12: 429-444.
57. Hetz C, Castilla J, Soto C (2007) Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J Biol Chem 282: 12725-12733.
58. Barria MA, Mukherjee A, Gonzalez-Romero D, Morales R, Soto C (2009) De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathog 5: e1000421.
59. Tang TS, Tu H, Chan EY, Maximov A, Wang Z, et al. (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39: 227-239.
60. Vidal R, Caballero B, Couve A, Hetz C (2011) Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease. Curr. Mol. Med, In press.
61. Soto C, Kascsak RJ, Saborio GP, Aucouturier P, Wisniewski T, et al. (2000) Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 355: 192-197.
62. Bosque PJ, Prusiner SB (2000) Cultured cell sublines highly susceptible to prion infection. J Virol 74: 4377-4386.
63. Enari M, Flechsig E, Weissmann C (2001) Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci U S A 98: 9295-9299.
64. Gleason MR, Armisen R, Verdecia MA, Sirotkin H, Brehm P, et al. (2004) A mutation in serca underlies motility dysfunction in accordion zebrafish. Dev Biol 276: 441-451.
65. 2+ mobilisation. Cell Physiol Biochem 20: 773-780.
66. Lisbona F, Rojas-Rivera D, Thielen P, Zamorano S, Todd D, et al. (2009) BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1alpha. Mol Cell 33: 679-691.