CoChat
Sign Up
Cited by 168Endoplasmic Reticulum Stress and DiseaseImmune Response and InflammationIon Channels and Receptors

Regulation of Cytokine Production by the Unfolded Protein Response; Implications for Infection and Autoimmunity

Open access
Smith, Judith A.·2018·Frontiers in Immunology
DOI 10.3389/fimmu.2018.00422PMC PMC5844972
Open this paper in CoChat — free accountOpen PDF

Abstract

Protein folding in the endoplasmic reticulum (ER) is an essential cell function. To safeguard this process in the face of environmental threats and internal stressors, cells mount an evolutionarily conserved response known as the unfolded protein response (UPR). Invading pathogens induce cellular stress that impacts protein folding, thus the UPR is well situated to sense danger and contribute to immune responses. Cytokines (inflammatory cytokines and interferons) critically mediate host defense against pathogens, but when aberrantly produced, may also drive pathologic inflammation. The UPR influences cytokine production on multiple levels, from stimulation of pattern recognition receptors, to modulation of inflammatory signaling pathways, and the regulation of cytokine transcription factors. This review will focus on the mechanisms underlying cytokine regulation by the UPR, and the repercussions of this relationship for infection and autoimmune/autoinflammatory diseases. Interrogation of viral and bacterial infections has revealed increasing numbers of examples where pathogens induce or modulate the UPR and implicated UPR-modulated cytokines in host response. The flip side of this coin, the UPR/ER stress responses have been increasingly recognized in a variety of autoimmune and inflammatory diseases. Examples include monogenic disorders of ER function, diseases linked to misfolding protein (HLA-B27 and spondyloarthritis), diseases directly implicating UPR and autophagy genes (inflammatory bowel disease), and autoimmune diseases targeting highly secretory cells (e.g., diabetes). Given the burgeoning interest in pharmacologically targeting the UPR, greater discernment is needed regarding how the UPR regulates cytokine production during specific infections and autoimmune processes, and the relative place of this interaction in pathogenesis.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3389/fimmu.2018.00422

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Chlamydia infection can induce cellular stress that impacts protein folding, thus inducing UPR activation; it is also proposed to modulate the UPR to promote its survival and replication.

    “Chlamydia infection can induce cellular stress that impacts protein folding, thus inducing UPR activation however it is also proposed to modulate the UPR to promote their survival and replication79.”

    From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [79]

    The 'Implications for Bacterial Infections' section (page not provided) reports that Chlamydia infection activates several ER-stress pathways, supporting the first part of the claim. It does not propose that Chlamydia modulates the UPR to promote its own survival or replication; the discussion of UPR-supported bacterial replication concerns Brucella. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 279

  1. [1]O’Brien C Flower DR Feighery C. Peptide length significantly influences in vitro affinity for MHC class II molecules. Immunome Res (2008) 4: 6. 10.1186/1745-7580-4-6 19036163 PMC2640366 · DOI
  2. [2]Calis JJ de Boer RJ Kesmir C. Degenerate T-cell recognition of peptides on MHC molecules creates large holes in the T-cell repertoire. PLoS Comput Biol (2012) 8(3): e1002412. 10.1371/journal.pcbi.1002412 22396638 PMC3291541 · DOI
  3. [3]Bremel RD Homan EJ Frequency patterns of T-cell exposed amino acid motifs in immunoglobulin heavy chain peptides presented by MHCs. Front Immunol (2014) 5: 541 10.3389/fimmu.2014.00541 25389426 PMC4211557 · DOI
  4. [5]Akira S Uematsu S Takeuchi O Pathogen recognition and innate immunity. Cell (2006) 124(4): 783– 801. 10.1016/j.cell.2006.02.015 16497588 · DOI
  5. [6]van Vliet SJ Garcia-Vallejo JJ van Kooyk Y. Dendritic cells and C-type lectin receptors: coupling innate to adaptive immune responses. Immunol Cell Biol (2008) 86(7): 580– 7. 10.1038/icb.2008.55 18679407 · DOI
  6. [7]Place DE Kanneganti TD. Recent advances in inflammasome biology. Curr Opin Immunol (2017) 50: 32– 8. 10.1016/j.coi.2017.10.011 29128729 PMC5857399 · DOI
  7. [8]Barber GN. STING-dependent cytosolic DNA sensing pathways. Trends Immunol (2014) 35(2): 88– 93. 10.1016/j.it.2013.10.010 24309426 · DOI
  8. [9]Rose NR. Negative selection, epitope mimicry and autoimmunity. Curr Opin Immunol (2017) 49: 51– 5. 10.1016/j.coi.2017.08.014 29102863 · DOI
  9. [10]Cunningham MW Post-streptococcal autoimmune sequelae: rheumatic fever and beyond. In: Ferretti JJ Stevens DL Fischetti VA, editors. Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. Oklahoma: University of Oklahoma Health Sciences Center (2016). 26866235
  10. [11]Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol (1994) 12: 991– 1045. 10.1146/annurev.iy.12.040194.005015 8011301 · DOI
  11. [12]Matzinger P. The danger model: a renewed sense of self. Science (2002) 296(5566): 301– 5. 10.1126/science.1071059 11951032 · DOI · Paper page
  12. [13]Pradeu T Cooper EL. The danger theory: 20 years later. Front Immunol (2012) 3: 287. 10.3389/fimmu.2012.00287 23060876 PMC3443751 · DOI
  13. [14]Land WG Agostinis P Gasser S Garg AD Linkermann A. Transplantation and damage-associated molecular patterns (DAMPs). Am J Transplant (2016) 16(12): 3338– 61. 10.1111/ajt.13963 27421829 · DOI
  14. [15]Kono H Rock KL How dying cells alert the immune system to danger. Nat Rev Immunol (2008) 8(4): 279– 89. 10.1038/nri2215 18340345 PMC2763408 · DOI · Paper page
  15. [16]Hirsiger S Simmen HP Werner CM Wanner GA Rittirsch D. Danger signals activating the immune response after trauma. Mediators Inflamm (2012) 2012: 315941. 10.1155/2012/315941 22778496 PMC3388465 · DOI
  16. [17]Yu L Wang L Chen S. Endogenous toll-like receptor ligands and their biological significance. J Cell Mol Med (2010) 14(11): 2592– 603. 10.1111/j.1582-4934.2010.01127.x 20629986 PMC4373479 · DOI
  17. [18]Erridge C. Endogenous ligands of TLR2 and TLR4: agonists or assistants? J Leukoc Biol (2010) 87(6): 989– 99. 10.1189/jlb.1209775 20179153 · DOI
  18. [19]Bhattacharyya S Varga J. Endogenous ligands of TLR4 promote unresolving tissue fibrosis: implications for systemic sclerosis and its targeted therapy. Immunol Lett (2018) 195: 9– 17. 10.1016/j.imlet.2017.09.011 28964818 PMC5820196 · DOI
  19. [20]Vance RE Isberg RR Portnoy DA. Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system. Cell Host Microbe (2009) 6(1): 10– 21. 10.1016/j.chom.2009.06.007 19616762 PMC2777727 · DOI
  20. [21]Karaolis DK Means TK Yang D Takahashi M Yoshimura T Muraille E Bacterial c-di-GMP is an immunostimulatory molecule. J Immunol (2007) 178(4): 2171– 81. 10.4049/jimmunol.178.4.2171 17277122 · DOI
  21. [22]Sun YH Rolan HG Tsolis RM. Injection of flagellin into the host cell cytosol by Salmonella enterica serotype typhimurium. J Biol Chem (2007) 282(47): 33897– 901. 10.1074/jbc.C700181200 17911114 · DOI
  22. [23]Lightfield KL Persson J Brubaker SW Witte CE von Moltke J Dunipace EA Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin. Nat Immunol (2008) 9(10): 1171– 8. 10.1038/ni.1646 18724372 PMC2614210 · DOI
  23. [24]Legrand-Poels S Kustermans G Bex F Kremmer E Kufer TA Piette J. Modulation of Nod2-dependent NF-kappaB signaling by the actin cytoskeleton. J Cell Sci (2007) 120(Pt 7): 1299– 310. 10.1242/jcs.03424 17356065 · DOI
  24. [25]Waite AL Schaner P Hu C Richards N Balci-Peynircioglu B Hong A Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin. Exp Biol Med (Maywood) (2009) 234(1): 40– 52. 10.3181/0806-RM-184 19109554 · DOI
  25. [26]Stevens FJ Argon Y. Protein folding in the ER. Semin Cell Dev Biol (1999) 10(5): 443– 54. 10.1006/scdb.1999.0315 10597627 · DOI
  26. [27]Schroder M Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem (2005) 74: 739– 89. 10.1146/annurev.biochem.73.011303.074134 15952902 · DOI
  27. [28]Harding HP Zeng H Zhang Y Jungries R Chung P Plesken H Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol Cell (2001) 7(6): 1153– 63. 10.1016/S1097-2765(01)00264-7 11430819 · DOI
  28. [29]Lee AH Chu GC Iwakoshi NN Glimcher LH. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J (2005) 24(24): 4368– 80. 10.1038/sj.emboj.7600903 16362047 PMC1356340 · DOI
  29. [30]Iwakoshi NN Lee AH Vallabhajosyula P Otipoby KL Rajewsky K Glimcher LH. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat Immunol (2003) 4(4): 321– 9. 10.1038/ni907 12612580 · DOI · Paper page
  30. [31]Shaffer AL Shapiro-Shelef M Iwakoshi NN Lee AH Qian SB Zhao H XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity (2004) 21(1): 81– 93. 10.1016/j.immuni.2004.06.010 15345222 · DOI
  31. [32]Todd DJ Lee AH Glimcher LH. The endoplasmic reticulum stress response in immunity and autoimmunity. Nat Rev Immunol (2008) 8(9): 663– 74. 10.1038/nri2359 18670423 · DOI
  32. [33]Iwakoshi NN Pypaert M Glimcher LH. The transcription factor XBP-1 is essential for the development and survival of dendritic cells. J Exp Med (2007) 204(10): 2267– 75. 10.1084/jem.20070525 17875675 PMC2118458 · DOI
  33. [34]Bettigole SE Lis R Adoro S Lee AH Spencer LA Weller PF The transcription factor XBP1 is selectively required for eosinophil differentiation. Nat Immunol (2015) 16(8): 829– 37. 10.1038/ni.3225 26147683 PMC4577297 · DOI
  34. [35]Grootjans J Kaser A Kaufman RJ Blumberg RS. The unfolded protein response in immunity and inflammation. Nat Rev Immunol (2016) 16(8): 469– 84. 10.1038/nri.2016.62 27346803 PMC5310224 · DOI
  35. [36]Oppenheim JJ. Cytokines: past, present, and future. Int J Hematol (2001) 74(1): 3– 8. 10.1007/BF02982543 11530802 · DOI
  36. [37]Zhang K Shen X Wu J Sakaki K Saunders T Rutkowski DT Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell (2006) 124(3): 587– 99. 10.1016/j.cell.2005.11.040 16469704 · DOI
  37. [38]Walter P Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science (2011) 334(6059): 1081– 6. 10.1126/science.1209038 22116877 · DOI
  38. [39]Credle JJ Finer-Moore JS Papa FR Stroud RM Walter P. On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc Natl Acad Sci U S A (2005) 102(52): 18773– 84. 10.1073/pnas.0509487102 16365312 PMC1316886 · DOI
  39. [40]Zhou J Liu CY Back SH Clark RL Peisach D Xu Z The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc Natl Acad Sci U S A (2006) 103(39): 14343– 8. 10.1073/pnas.0606480103 16973740 PMC1566190 · DOI
  40. [41]Karagöz GE Acosta-Alvear D Nguyen HT Lee CP Chu F Walter P. An unfolded protein-induced conformational switch activates mammalian IRE1. Elife (2017) 6: e30700. 10.7554/eLife.30700 28971800 PMC5699868 · DOI
  41. [42]Volmer R van der Ploeg K Ron D. Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc Natl Acad Sci U S A (2013) 110(12): 4628– 33. 10.1073/pnas.1217611110 23487760 PMC3606975 · DOI
  42. [43]Bertolotti A Wang X Novoa I Jungreis R Schlessinger K Cho JH Increased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient mice. J Clin Invest (2001) 107(5): 585– 93. 10.1172/JCI11476 11238559 PMC199427 · DOI
  43. [44]Martino MB Jones L Brighton B Ehre C Abdulah L Davis CW The ER stress transducer IRE1beta is required for airway epithelial mucin production. Mucosal Immunol (2013) 6(3): 639– 54. 10.1038/mi.2012.105 23168839 PMC4031691 · DOI
  44. [45]Hetz C Martinon F Rodriguez D Glimcher LH The unfolded protein response: integrating stress signals through the stress sensor IRE1alpha. Physiol Rev (2011) 91(4): 1219– 43. 10.1152/physrev.00001.2011 22013210 · DOI
  45. [46]Lee AH Iwakoshi NN Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol (2003) 23(21): 7448– 59. 10.1128/MCB.23.21.7448-7459.2003 14559994 PMC207643 · DOI
  46. [47]Sriburi R Bommiasamy H Buldak GL Robbins GR Frank M Jackowski S Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis. J Biol Chem (2007) 282(10): 7024– 34. 10.1074/jbc.M609490200 17213183 · DOI
  47. [48]Jäger R Bertrand MJ Gorman AM Vandenabeele P Samali A. The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress. Biol Cell (2012) 104(5): 259– 70. 10.1111/boc.201100055 22268789 · DOI
  48. [49]Lin JH Li H Yasumura D Cohen HR Zhang C Panning B IRE1 signaling affects cell fate during the unfolded protein response. Science (2007) 318(5852): 944– 9. 10.1126/science.1146361 17991856 PMC3670588 · DOI
  49. [50]Hollien J Weissman JS. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science (2006) 313(5783): 104– 7. 10.1126/science.1129631 16825573 · DOI
  50. [51]Hollien J Lin JH Li H Stevens N Walter P Weissman JS. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol (2009) 186(3): 323– 31. 10.1083/jcb.200903014 19651891 PMC2728407 · DOI
  51. [52]Han D Lerner AG Vande Walle L Upton JP Xu W Hagen A IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell (2009) 138(3): 562– 75. 10.1016/j.cell.2009.07.017 19665977 PMC2762408 · DOI
  52. [53]Ghosh R Wang L Wang ES Perera BG Igbaria A Morita S Allosteric inhibition of the IRE1alpha RNase preserves cell viability and function during endoplasmic reticulum stress. Cell (2014) 158(3): 534– 48. 10.1016/j.cell.2014.07.002 25018104 PMC4244221 · DOI
  53. [54]Hetz C Glimcher LH. Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol Cell (2009) 35(5): 551– 61. 10.1016/j.molcel.2009.08.021 19748352 PMC3101568 · DOI
  54. [55]Nishitoh H Matsuzawa A Tobiume K Saegusa K Takeda K Inoue K ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev (2002) 16(11): 1345– 55. 10.1101/gad.992302 12050113 PMC186318 · DOI
  55. [56]Hetz C Bernasconi P Fisher J Lee AH Bassik MC Antonsson B Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Science (2006) 312(5773): 572– 6. 10.1126/science.1123480 16645094 · DOI
  56. [57]Young SK Palam LR Wu C Sachs MS Wek RC. Ribosome elongation stall directs gene-specific translation in the integrated stress response. J Biol Chem (2016) 291(12): 6546– 58. 10.1074/jbc.M115.705640 26817837 PMC4813566 · DOI
  57. [58]Harding HP Zhang Y Bertolotti A Zeng H Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell (2000) 5(5): 897– 904. 10.1016/S1097-2765(00)80330-5 10882126 · DOI · Paper page
  58. [59]Lu PD Harding HP Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol (2004) 167(1): 27– 33. 10.1083/jcb.200408003 15479734 PMC2172506 · DOI · Paper page
  59. [60]Vattem KM Wek RC. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci U S A (2004) 101(31): 11269– 74. 10.1073/pnas.0400541101 15277680 PMC509193 · DOI · Paper page
  60. [61]Harding HP Zhang Y Zeng H Novoa I Lu PD Calfon M An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell (2003) 11(3): 619– 33. 10.1016/S1097-2765(03)00105-9 12667446 · DOI
  61. [62]B’Chir W Maurin AC Carraro V Averous J Jousse C Muranishi Y The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression. Nucleic Acids Res (2013) 41(16): 7683– 99. 10.1093/nar/gkt563 23804767 PMC3763548 · DOI · Paper page
  62. [63]Novoa I Zeng H Harding HP Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol (2001) 153(5): 1011– 22. 10.1083/jcb.153.5.1011 11381086 PMC2174339 · DOI
  63. [64]Yan W Frank CL Korth MJ Sopher BL Novoa I Ron D Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci U S A (2002) 99(25): 15920– 5. 10.1073/pnas.252341799 12446838 PMC138540 · DOI · Paper page
  64. [65]Zhang HM Ye X Su Y Yuan J Liu Z Stein DA Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1. J Virol (2010) 84(17): 8446– 59. 10.1128/JVI.01416-09 20554776 PMC2918999 · DOI
  65. [66]Jousse C Oyadomari S Novoa I Lu P Zhang Y Harding HP Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells. J Cell Biol (2003) 163(4): 767– 75. 10.1083/jcb.200308075 14638860 PMC2173671 · DOI
  66. [67]Pakos-Zebrucka K Koryga I Mnich K Ljujic M Samali A Gorman AM. The integrated stress response. EMBO Rep (2016) 17(10): 1374– 95. 10.15252/embr.201642195 27629041 PMC5048378 · DOI · Paper page
  67. [68]Cullinan SB Zhang D Hannink M Arvisais E Kaufman RJ Diehl JA. Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol Cell Biol (2003) 23(20): 7198– 209. 10.1128/MCB.23.20.7198-7209.2003 14517290 PMC230321 · DOI
  68. [69]Shen J Chen X Hendershot L Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell (2002) 3(1): 99– 111. 10.1016/S1534-5807(02)00203-4 12110171 · DOI
  69. [70]Yamamoto K Sato T Matsui T Sato M Okada T Yoshida H Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell (2007) 13(3): 365– 76. 10.1016/j.devcel.2007.07.018 17765680 · DOI
  70. [71]Lee K Tirasophon W Shen X Michalak M Prywes R Okada T IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev (2002) 16(4): 452– 66. 10.1101/gad.964702 11850408 PMC155339 · DOI
  71. [72]Asada R Kanemoto S Kondo S Saito A Imaizumi K. The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology. J Biochem (2011) 149(5): 507– 18. 10.1093/jb/mvr041 21454302 · DOI
  72. [74]Martinon F Chen X Lee AH Glimcher LH. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat Immunol (2010) 11(5): 411– 8. 10.1038/ni.1857 20351694 PMC3113706 · DOI · Paper page
  73. [75]Peters LR Raghavan M. Endoplasmic reticulum calcium depletion impacts chaperone secretion, innate immunity, and phagocytic uptake of cells. J Immunol (2011) 187(2): 919– 31. 10.4049/jimmunol.1100690 21670312 PMC3371385 · DOI
  74. [76]Hayden MS Ghosh S. Shared principles in NF-kappaB signaling. Cell (2008) 132(3): 344– 62. 10.1016/j.cell.2008.01.020 18267068 · DOI
  75. [77]Hu P Han Z Couvillon AD Kaufman RJ Exton JH. Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol Cell Biol (2006) 26(8): 3071– 84. 10.1128/MCB.26.8.3071-3084.2006 16581782 PMC1446932 · DOI
  76. [78]Kaneko M Niinuma Y Nomura Y. Activation signal of nuclear factor-kappa B in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2. Biol Pharm Bull (2003) 26(7): 931– 5. 10.1248/bpb.26.931 12843613 · DOI
  77. [79]Tam AB Mercado EL Hoffmann A Niwa M ER stress activates NF-kappaB by integrating functions of basal IKK activity, IRE1 and PERK. PLoS One (2012) 7(10): e45078 10.1371/journal.pone.0045078 23110043 PMC3482226 · DOI
  78. [80]Kim S Joe Y Kim HJ Kim YS Jeong SO Pae HO Endoplasmic reticulum stress-induced IRE1alpha activation mediates cross-talk of GSK-3beta and XBP-1 to regulate inflammatory cytokine production. J Immunol (2015) 194(9): 4498– 506. 10.4049/jimmunol.1401399 25821218 PMC4400814 · DOI
  79. [81]Demarchi F Bertoli C Sandy P Schneider C. Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability. J Biol Chem (2003) 278(41): 39583– 90. 10.1074/jbc.M305676200 12871932 · DOI
  80. [82]Deng J Lu PD Zhang Y Scheuner D Kaufman RJ Sonenberg N Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol Cell Biol (2004) 24(23): 10161– 8. 10.1128/MCB.24.23.10161-10168.2004 15542827 PMC529034 · DOI
  81. [83]Park SH Choi HJ Yang H Do KH Kim J Lee DW Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma. J Biol Chem (2010) 285(46): 35330– 9. 10.1074/jbc.M110.136259 20829347 PMC2975157 · DOI
  82. [84]Yamazaki H Hiramatsu N Hayakawa K Tagawa Y Okamura M Ogata R Activation of the Akt-NF-kappaB pathway by subtilase cytotoxin through the ATF6 branch of the unfolded protein response. J Immunol (2009) 183(2): 1480– 7. 10.4049/jimmunol.0900017 19561103 PMC2762936 · DOI
  83. [85]Nakajima S Hiramatsu N Hayakawa K Saito Y Kato H Huang T Selective abrogation of BiP/GRP78 blunts activation of NF-kappaB through the ATF6 branch of the UPR: involvement of C/EBPbeta and mTOR-dependent dephosphorylation of Akt. Mol Cell Biol (2011) 31(8): 1710– 8. 10.1128/MCB.00939-10 21300786 PMC3126329 · DOI
  84. [86]Pahl HL Baeuerle PA. Activation of NF-kappa B by ER stress requires both Ca2+ and reactive oxygen intermediates as messengers. FEBS Lett (1996) 392(2): 129– 36. 10.1016/0014-5793(96)00800-9 8772190 · DOI
  85. [88]Darling NJ Cook SJ. The role of MAPK signalling pathways in the response to endoplasmic reticulum stress. Biochim Biophys Acta (2014) 1843(10): 2150– 63. 10.1016/j.bbamcr.2014.01.009 24440275 · DOI
  86. [89]Ichijo H Nishida E Irie K ten Dijke P Saitoh M Moriguchi T Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science (1997) 275(5296): 90– 4. 10.1126/science.275.5296.90 8974401 · DOI
  87. [90]Nguyên DT Kebache S Fazel A Wong HN Jenna S Emadali A Nck-dependent activation of extracellular signal-regulated kinase-1 and regulation of cell survival during endoplasmic reticulum stress. Mol Biol Cell (2004) 15(9): 4248– 60. 10.1091/mbc.E03-11-0851 15201339 PMC515356 · DOI
  88. [91]Mijošek V Lasitschka F Warth A Zabeck H Dalpke AH Weitnauer M. Endoplasmic reticulum stress is a danger signal promoting innate inflammatory responses in bronchial epithelial cells. J Innate Immun (2016) 8(5): 464– 78. 10.1159/000447668 27423489 PMC6738801 · DOI
  89. [92]Wang XZ Ron D. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science (1996) 272(5266): 1347– 9. 10.1126/science.272.5266.1347 8650547 · DOI
  90. [93]Luo S Lee AS. Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target for stress-induced phosphorylation. Biochem J (2002) 366(Pt 3): 787– 95. 10.1042/BJ20011802 12076252 PMC1222838 · DOI
  91. [94]Thuerauf DJ Arnold ND Zechner D Hanford DS DeMartin KM McDonough PM p38 Mitogen-activated protein kinase mediates the transcriptional induction of the atrial natriuretic factor gene through a serum response element. A potential role for the transcription factor ATF6. J Biol Chem (1998) 273(32): 20636– 43. 10.1074/jbc.273.32.20636 9685422 · DOI
  92. [95]Sato M Suemori H Hata N Asagiri M Ogasawara K Nakao K Distinct and essential roles of transcription factors IRF-3 and IRF-7 in response to viruses for IFN-alpha/beta gene induction. Immunity (2000) 13(4): 539– 48. 10.1016/S1074-7613(00)00053-4 11070172 · DOI
  93. [96]Agalioti T Lomvardas S Parekh B Yie J Maniatis T Thanos D. Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter. Cell (2000) 103(4): 667– 78. 10.1016/S0092-8674(00)00169-0 11106736 · DOI
  94. [97]Merika M Thanos D. Enhanceosomes. Curr Opin Genet Dev (2001) 11(2): 205– 8. 10.1016/S0959-437X(00)00180-5 11250145 · DOI
  95. [98]Panne D Maniatis T Harrison SC. An atomic model of the interferon-beta enhanceosome. Cell (2007) 129(6): 1111– 23. 10.1016/j.cell.2007.05.019 17574024 PMC2020837 · DOI · Paper page
  96. [99]Hiscott J. Triggering the innate antiviral response through IRF-3 activation. J Biol Chem (2007) 282(21): 15325– 9. 10.1074/jbc.R700002200 17395583 · DOI
  97. [100]Chen W Srinath H Lam SS Schiffer CA Royer WE Jr Lin K. Contribution of Ser386 and Ser396 to activation of interferon regulatory factor 3. J Mol Biol (2008) 379(2): 251– 60. 10.1016/j.jmb.2008.03.050 18440553 PMC2410038 · DOI
  98. [101]Liu YP Zeng L Tian A Bomkamp A Rivera D Gutman D Endoplasmic reticulum stress regulates the innate immunity critical transcription factor IRF3. J Immunol (2012) 189(9): 4630– 9. 10.4049/jimmunol.1102737 23028052 PMC3478468 · DOI
  99. [102]Zeng L Liu YP Sha H Chen H Qi L Smith JA. XBP-1 couples endoplasmic reticulum stress to augmented IFN-beta induction via a cis-acting enhancer in macrophages. J Immunol (2010) 185(4): 2324– 30. 10.4049/jimmunol.0903052 20660350 PMC2916979 · DOI
  100. [103]Iwasaki Y Suganami T Hachiya R Shirakawa I Kim-Saijo M Tanaka M Activating transcription factor 4 links metabolic stress to interleukin-6 expression in macrophages. Diabetes (2014) 63(1): 152– 61. 10.2337/db13-0757 23990363 · DOI
  101. [104]Goodall JC Wu C Zhang Y McNeill L Ellis L Saudek V Endoplasmic reticulum stress-induced transcription factor, CHOP, is crucial for dendritic cell IL-23 expression. Proc Natl Acad Sci U S A (2010) 107(41): 17698– 703. 10.1073/pnas.1011736107 20876114 PMC2955096 · DOI
  102. [105]Jiang HY Wek SA McGrath BC Lu D Hai T Harding HP Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response. Mol Cell Biol (2004) 24(3): 1365– 77. 10.1128/MCB.24.3.1365-1377.2004 14729979 PMC321431 · DOI
  103. [106]Brooks AC Guo Y Singh M McCracken J Xuan YT Srivastava S Endoplasmic reticulum stress-dependent activation of ATF3 mediates the late phase of ischemic preconditioning. J Mol Cell Cardiol (2014) 76: 138– 47. 10.1016/j.yjmcc.2014.08.011 25151953 PMC4336548 · DOI
  104. [107]Gilchrist M Thorsson V Li B Rust AG Korb M Roach JC Systems biology approaches identify ATF3 as a negative regulator of Toll-like receptor 4. Nature (2006) 441(7090): 173– 8. 10.1038/nature04768 16688168 · DOI
  105. [108]Whitmore MM Iparraguirre A Kubelka L Weninger W Hai T Williams BR. Negative regulation of TLR-signaling pathways by activating transcription factor-3. J Immunol (2007) 179(6): 3622– 30. 10.4049/jimmunol.179.6.3622 17785797 · DOI
  106. [109]Thompson MR Xu D Williams BR. ATF3 transcription factor and its emerging roles in immunity and cancer. J Mol Med (Berl) (2009) 87(11): 1053– 60. 10.1007/s00109-009-0520-x 19705082 PMC2783469 · DOI
  107. [110]Dong D Fu N Yang P. MiR-17 downregulation by high glucose stabilizes thioredoxin-interacting protein and removes thioredoxin inhibition on ASK1 leading to apoptosis. Toxicol Sci (2016) 150(1): 84– 96. 10.1093/toxsci/kfv313 26660634 PMC4830238 · DOI
  108. [111]Lerner AG Upton JP Praveen PV Ghosh R Nakagawa Y Igbaria A IRE1alpha induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress. Cell Metab (2012) 16(2): 250– 64. 10.1016/j.cmet.2012.07.007 22883233 PMC4014071 · DOI
  109. [112]Oslowski CM Hara T O’Sullivan-Murphy B Kanekura K Lu S Hara M Thioredoxin-interacting protein mediates ER stress-induced beta cell death through initiation of the inflammasome. Cell Metab (2012) 16(2): 265– 73. 10.1016/j.cmet.2012.07.005 22883234 PMC3418541 · DOI
  110. [113]Bronner DN Abuaita BH Chen X Fitzgerald KA Nuñez G He Y Endoplasmic reticulum stress activates the inflammasome via NLRP3- and caspase-2-driven mitochondrial damage. Immunity (2015) 43(3): 451– 62. 10.1016/j.immuni.2015.08.008 26341399 PMC4582788 · DOI
  111. [114]Cho HK Cheong KJ Kim HY Cheong J. Endoplasmic reticulum stress induced by hepatitis B virus X protein enhances cyclo-oxygenase 2 expression via activating transcription factor 4. Biochem J (2011) 435(2): 431– 9. 10.1042/BJ20102071 21244365 · DOI
  112. [115]West AP Khoury-Hanold W Staron M Tal MC Pineda CM Lang SM Mitochondrial DNA stress primes the antiviral innate immune response. Nature (2015) 520(7548): 553– 7. 10.1038/nature14156 25642965 PMC4409480 · DOI · Paper page
  113. [116]Cao SS Kaufman RJ. Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease. Antioxid Redox Signal (2014) 21(3): 396– 413. 10.1089/ars.2014.5851 24702237 PMC4076992 · DOI
  114. [117]Szabadkai G Bianchi K Várnai P De Stefani D Wieckowski MR Cavagna D Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels. J Cell Biol (2006) 175(6): 901– 11. 10.1083/jcb.200608073 17178908 PMC2064700 · DOI · Paper page
  115. [118]Keestra-Gounder AM Byndloss MX Seyffert N Young BM Chávez-Arroyo A Tsai AY NOD1 and NOD2 signalling links ER stress with inflammation. Nature (2016) 532(7599): 394– 7. 10.1038/nature17631 27007849 PMC4869892 · DOI
  116. [119]Xie P. TRAF molecules in cell signaling and in human diseases. J Mol Signal (2013) 8(1): 7. 10.1186/1750-2187-8-7 23758787 PMC3697994 · DOI
  117. [120]Smith JA Turner MJ DeLay ML Klenk EI Sowders DP Colbert RA. Endoplasmic reticulum stress and the unfolded protein response are linked to synergistic IFN-beta induction via X-box binding protein 1. Eur J Immunol (2008) 38(5): 1194– 203. 10.1002/eji.200737882 18412159 PMC2838478 · DOI
  118. [121]DeLay ML Turner MJ Klenk EI Smith JA Sowders DP Colbert RA. HLA-B27 misfolding and the unfolded protein response augment interleukin-23 production and are associated with Th17 activation in transgenic rats. Arthritis Rheum (2009) 60(9): 2633– 43. 10.1002/art.24763 19714651 PMC2893331 · DOI
  119. [122]Hu F Yu X Wang H Zuo D Guo C Yi H ER stress and its regulator X-box-binding protein-1 enhance polyIC-induced innate immune response in dendritic cells. Eur J Immunol (2011) 41(4): 1086– 97. 10.1002/eji.201040831 21400498 PMC3157298 · DOI
  120. [123]Shenderov K Riteau N Yip R Mayer-Barber KD Oland S Hieny S Cutting edge: endoplasmic reticulum stress licenses macrophages to produce mature IL-1beta in response to TLR4 stimulation through a caspase-8- and TRIF-dependent pathway. J Immunol (2014) 192(5): 2029– 33. 10.4049/jimmunol.1302549 24489101 PMC3935725 · DOI
  121. [124]Leonard A Paton AW El-Quadi M Paton JC Fazal F. Preconditioning with endoplasmic reticulum stress ameliorates endothelial cell inflammation. PLoS One (2014) 9(10): e110949. 10.1371/journal.pone.0110949 25356743 PMC4214695 · DOI
  122. [125]Woo CW Cui D Arellano J Dorweiler B Harding H Fitzgerald KA Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling. Nat Cell Biol (2009) 11(12): 1473– 80. 10.1038/ncb1996 19855386 PMC2787632 · DOI
  123. [126]Nakayama Y Endo M Tsukano H Mori M Oike Y Gotoh T. Molecular mechanisms of the LPS-induced non-apoptotic ER stress-CHOP pathway. J Biochem (2010) 147(4): 471– 83. 10.1093/jb/mvp189 19919955 · DOI
  124. [127]Clavarino G Cláudio N Couderc T Dalet A Judith D Camosseto V Induction of GADD34 is necessary for dsRNA-dependent interferon-beta production and participates in the control of chikungunya virus infection. PLoS Pathog (2012) 8(5): e1002708 10.1371/journal.ppat.1002708 22615568 PMC3355096 · DOI
  125. [128]Clavarino G Cláudio N Dalet A Terawaki S Couderc T Chasson L Protein phosphatase 1 subunit Ppp1r15a/GADD34 regulates cytokine production in polyinosinic:polycytidylic acid-stimulated dendritic cells. Proc Natl Acad Sci U S A (2012) 109(8): 3006– 11. 10.1073/pnas.1104491109 22315398 PMC3286954 · DOI
  126. [129]Cláudio N Dalet A Gatti E Pierre P. Mapping the crossroads of immune activation and cellular stress response pathways. EMBO J (2013) 32(9): 1214– 24. 10.1038/emboj.2013.80 23584529 PMC3642686 · DOI
  127. [130]Obeid M Tesniere A Ghiringhelli F Fimia GM Apetoh L Perfettini JL Calreticulin exposure dictates the immunogenicity of cancer cell death. Nat Med (2007) 13(1): 54– 61. 10.1038/nm1523 17187072 · DOI · Paper page
  128. [131]Galluzzi L Diotallevi A Magnani M. Endoplasmic reticulum stress and unfolded protein response in infection by intracellular parasites. Future Sci OA (2017) 3(3): FSO198. 10.4155/fsoa-2017-0020 28883998 PMC5583660 · DOI
  129. [132]Ren J Liu T Pang L Li K Garofalo RP Casola A A novel mechanism for the inhibition of interferon regulatory factor-3-dependent gene expression by human respiratory syncytial virus NS1 protein. J Gen Virol (2011) 92(Pt 9): 2153– 9. 10.1099/vir.0.032987-0 21632562 PMC3353388 · DOI
  130. [133]Nitta S Sakamoto N Nakagawa M Kakinuma S Mishima K Kusano-Kitazume A Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity. Hepatology (2013) 57(1): 46– 58. 10.1002/hep.26017 22911572 · DOI
  131. [134]Sun L Xing Y Chen X Zheng Y Yang Y Nichols DB Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling. PLoS One (2012) 7(2): e30802. 10.1371/journal.pone.0030802 22312431 PMC3270028 · DOI
  132. [135]Aguirre S Maestre AM Pagni S Patel JR Savage T Gutman D DENV inhibits type I IFN production in infected cells by cleaving human STING. PLoS Pathog (2012) 8(10): e1002934. 10.1371/journal.ppat.1002934 23055924 PMC3464218 · DOI
  133. [136]Aguirre S Luthra P Sanchez-Aparicio MT Maestre AM Patel J Lamothe F Dengue virus NS2B protein targets cGAS for degradation and prevents mitochondrial DNA sensing during infection. Nat Microbiol (2017) 2: 17037. 10.1038/nmicrobiol.2017.37 28346446 PMC7457382 · DOI
  134. [137]Liu J HuangFu WC Kumar KG Qian J Casey JP Hamanaka RB Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor. Cell Host Microbe (2009) 5(1): 72– 83. 10.1016/j.chom.2008.11.008 19154989 PMC2741731 · DOI
  135. [138]Horvath CM Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein. Eur J Biochem (2004) 271(23–24): 4621– 8. 10.1111/j.1432-1033.2004.04425.x 15606749 · DOI
  136. [139]Choe SS Dodd DA Kirkegaard K. Inhibition of cellular protein secretion by picornaviral 3A proteins. Virology (2005) 337(1): 18– 29. 10.1016/j.virol.2005.03.036 15914217 · DOI
  137. [140]Moradpour D Penin F Rice CM. Replication of hepatitis C virus. Nat Rev Microbiol (2007) 5(6): 453– 63. 10.1038/nrmicro1645 17487147 · DOI
  138. [141]Romero-Brey I Merz A Chiramel A Lee JY Chlanda P Haselman U Three-dimensional architecture and biogenesis of membrane structures associated with hepatitis C virus replication. PLoS Pathog (2012) 8(12): e1003056. 10.1371/journal.ppat.1003056 23236278 PMC3516559 · DOI
  139. [142]Knoops K Kikkert M Worm SH Zevenhoven-Dobbe JC van der Meer Y Koster AJ SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol (2008) 6(9): e226. 10.1371/journal.pbio.0060226 18798692 PMC2535663 · DOI
  140. [143]Li S Kong L Yu X. The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis. Crit Rev Microbiol (2015) 41(2): 150– 64. 10.3109/1040841X.2013.813899 25168431 PMC7113905 · DOI
  141. [144]Zhang L Wang A. Virus-induced ER stress and the unfolded protein response. Front Plant Sci (2012) 3: 293. 10.3389/fpls.2012.00293 23293645 PMC3531707 · DOI
  142. [145]Pena J Harris E Dengue virus modulates the unfolded protein response in a time-dependent manner. J Biol Chem (2011) 286(16): 14226– 36. 10.1074/jbc.M111.222703 21385877 PMC3077624 · DOI
  143. [146]Zheng Y Gao B Ye L Kong L Jing W Yang X Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response. J Microbiol (2005) 43(6): 529– 36. 16410770
  144. [147]Chan SW Egan PA. Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J (2005) 19(11): 1510– 2. 10.1096/fj.04-3455fje 16006626 · DOI
  145. [148]Lee DY Sugden B. The LMP1 oncogene of EBV activates PERK and the unfolded protein response to drive its own synthesis. Blood (2008) 111(4): 2280– 9. 10.1182/blood-2007-07-100032 18042799 PMC2234060 · DOI
  146. [149]Li B Gao B Ye L Han X Wang W Kong L Hepatitis B virus X protein (HBx) activates ATF6 and IRE1-XBP1 pathways of unfolded protein response. Virus Res (2007) 124(1–2): 44– 9. 10.1016/j.virusres.2006.09.011 17092596 · DOI
  147. [150]Chan CP Siu KL Chin KT Yuen KY Zheng B Jin DY. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J Virol (2006) 80(18): 9279– 87. 10.1128/JVI.80.7.3225-3237.2006 16940539 PMC1563899 · DOI
  148. [151]Roberson EC Tully JE Guala AS Reiss JN Godburn KE Pociask DA Influenza induces endoplasmic reticulum stress, caspase-12-dependent apoptosis, and c-Jun N-terminal kinase-mediated transforming growth factor-beta release in lung epithelial cells. Am J Respir Cell Mol Biol (2012) 46(5): 573– 81. 10.1165/rcmb.2010-0460OC 21799120 PMC3359902 · DOI
  149. [152]Rathore AP Ng ML Vasudevan SG Differential unfolded protein response during chikungunya and sindbis virus infection: CHIKV nsP4 suppresses eIF2alpha phosphorylation. Virol J (2013) 10: 36 10.1186/1743-422X-10-36 23356742 PMC3605262 · DOI
  150. [153]Pasqual G Burri DJ Pasquato A de la Torre JC Kunz S. Role of the host cell’s unfolded protein response in arenavirus infection. J Virol (2011) 85(4): 1662– 70. 10.1128/JVI.01782-10 21106748 PMC3028902 · DOI
  151. [154]He B Gross M Roizman B. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc Natl Acad Sci U S A (1997) 94(3): 843– 8. 9023344 PMC19601
  152. [155]Cheng G Brett ME He B. Val193 and Phe195 of the gamma 1 34.5 protein of herpes simplex virus 1 are required for viral resistance to interferon-alpha/beta. Virology (2001) 290(1): 115– 20. 10.1006/viro.2001.1148 11882996 · DOI
  153. [156]Zhang F Moon A Childs K Goodbourn S Dixon LK. The African swine fever virus DP71L protein recruits the protein phosphatase 1 catalytic subunit to dephosphorylate eIF2alpha and inhibits CHOP induction but is dispensable for these activities during virus infection. J Virol (2010) 84(20): 10681– 9. 10.1128/JVI.01027-10 20702639 PMC2950568 · DOI
  154. [157]Bhattacharyya S Sen U Vrati S. Regulated IRE1-dependent decay pathway is activated during Japanese encephalitis virus-induced unfolded protein response and benefits viral replication. J Gen Virol (2014) 95(Pt 1): 71– 9. 10.1099/vir.0.057265-0 24114795 · DOI
  155. [158]Zhang P Su C Jiang Z Zheng C. Herpes simplex virus 1 UL41 protein suppresses the IRE1/XBP1 signal pathway of the unfolded protein response via Its RNase activity. J Virol (2017) 91(4): e2056– 2016. 10.1128/JVI.02056-16 27928013 PMC5286897 · DOI
  156. [159]Tardif KD Mori K Kaufman RJ Siddiqui A. Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J Biol Chem (2004) 279(17): 17158– 64. 10.1074/jbc.M312144200 14960590 · DOI
  157. [160]Hassan IH Zhang MS Powers LS Shao JQ Baltrusaitis J Rutkowski DT Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J Biol Chem (2012) 287(7): 4679– 89. 10.1074/jbc.M111.284695 22194594 PMC3281634 · DOI
  158. [161]Fraser JE Wang C Chan KW Vasudevan SG Jans DA Novel dengue virus inhibitor 4-HPR activates ATF4 independent of protein kinase R-like endoplasmic reticulum kinase and elevates levels of eIF2alpha phosphorylation in virus infected cells. Antiviral Res (2016) 130: 1– 6. 10.1016/j.antiviral.2016.03.006 26965420 · DOI
  159. [162]Medigeshi GR Lancaster AM Hirsch AJ Briese T Lipkin WI Defilippis V West nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis. J Virol (2007) 81(20): 10849– 60. 10.1128/JVI.01151-07 17686866 PMC2045561 · DOI
  160. [163]Jiang G Santos Rocha C Hirao LA Mendes EA Tang Y Thompson GR III HIV exploits antiviral host innate GCN2-ATF4 signaling for establishing viral replication early in infection. MBio (2017) 8(3): e1518– 1516. 10.1128/mBio.01518-16 28465428 PMC5414007 · DOI
  161. [164]Diwaker D Mishra KP Ganju L. Effect of modulation of unfolded protein response pathway on dengue virus infection. Acta Biochim Biophys Sin (Shanghai) (2015) 47(12): 960– 8. 10.1093/abbs/gmv108 26515795 · DOI
  162. [165]Cheng YL Lin YS Chen CL Tsai TT Tsai CC Wu YW Activation of Nrf2 by the dengue virus causes an increase in CLEC5A, which enhances TNF-alpha production by mononuclear phagocytes. Sci Rep (2016) 6: 32000 10.1038/srep32000 27561946 PMC4999957 · DOI
  163. [166]Ke PY Chen SS. Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro. J Clin Invest (2011) 121(1): 37– 56. 10.1172/JCI41474 21135505 PMC3007134 · DOI
  164. [167]Wolfson JJ May KL Thorpe CM Jandhyala DM Paton JC Paton AW. Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways. Cell Microbiol (2008) 10(9): 1775– 86. 10.1111/j.1462-5822.2008.01164.x 18433465 PMC2575110 · DOI
  165. [168]Paton AW Srimanote P Talbot UM Wang H Paton JC. A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli. J Exp Med (2004) 200(1): 35– 46. 10.1084/jem.20040392 15226357 PMC2213318 · DOI
  166. [169]Harama D Koyama K Mukai M Shimokawa N Miyata M Nakamura Y A subcytotoxic dose of subtilase cytotoxin prevents lipopolysaccharide-induced inflammatory responses, depending on its capacity to induce the unfolded protein response. J Immunol (2009) 183(2): 1368– 74. 10.4049/jimmunol.0804066 19553530 · DOI
  167. [170]Lee SY Lee MS Cherla RP Tesh VL. Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells. Cell Microbiol (2008) 10(3): 770– 80. 10.1111/j.1462-5822.2007.01083.x 18005243 · DOI
  168. [171]Pillich H Loose M Zimmer KP Chakraborty T. Activation of the unfolded protein response by Listeria monocytogenes. Cell Microbiol (2012) 14(6): 949– 64. 10.1111/j.1462-5822.2012.01769.x 22321539 · DOI
  169. [172]Gekara NO Groebe L Viegas N Weiss S. Listeria monocytogenes desensitizes immune cells to subsequent Ca2+ signaling via listeriolysin O-induced depletion of intracellular Ca2+ stores. Infect Immun (2008) 76(2): 857– 62. 10.1128/IAI.00622-07 18056478 PMC2223449 · DOI
  170. [173]Cho JA Lee AH Platzer B Cross BC Gardner BM De Luca H The unfolded protein response element IRE1alpha senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling. Cell Host Microbe (2013) 13(5): 558– 69. 10.1016/j.chom.2013.03.011 23684307 PMC3766372 · DOI
  171. [174]de Jong MF Starr T Winter MG den Hartigh AB Child R Knodler LA Sensing of bacterial type IV secretion via the unfolded protein response. MBio (2013) 4(1): e418– 412. 10.1128/mBio.00418-12 23422410 PMC3624511 · DOI
  172. [175]Myeni S Child R Ng TW Kupko JJ III Wehrly TD Porcella SF Brucella modulates secretory trafficking via multiple type IV secretion effector proteins. PLoS Pathog (2013) 9(8): e1003556. 10.1371/journal.ppat.1003556 23950720 PMC3738490 · DOI
  173. [176]Celli J de Chastellier C Franchini DM Pizarro-Cerda J Moreno E Gorvel JP. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J Exp Med (2003) 198(4): 545– 56. 10.1084/jem.20030088 12925673 PMC2194179 · DOI
  174. [177]Tilney LG Harb OS Connelly PS Robinson CG Roy CR. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. J Cell Sci (2001) 114(Pt 24): 4637– 50. 11792828
  175. [178]Derre I Swiss R Agaisse H. The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sites. PLoS Pathog (2011) 7(6): e1002092. 10.1371/journal.ppat.1002092 21731489 PMC3121800 · DOI
  176. [179]Shima K Klinger M Schütze S Kaufhold I Solbach W Reiling N The role of endoplasmic reticulum-related BiP/GRP78 in interferon gamma-induced persistent Chlamydia pneumoniae infection. Cell Microbiol (2015) 17(7): 923– 34. 10.1111/cmi.12416 25588955 · DOI
  177. [180]Webster SJ Ellis L O’Brien LM Tyrrell B Fitzmaurice TJ Elder MJ IRE1alpha mediates PKR activation in response to Chlamydia trachomatis infection. Microbes Infect (2016) 18(7–8): 472– 83. 10.1016/j.micinf.2016.03.010 27021640 PMC4936793 · DOI
  178. [181]Hempstead AD Isberg RR. Inhibition of host cell translation elongation by Legionella pneumophila blocks the host cell unfolded protein response. Proc Natl Acad Sci U S A (2015) 112(49): E6790– 7. 10.1073/pnas.1508716112 26598709 PMC4679008 · DOI
  179. [182]Smith JA Khan M Magnani DD Harms JS Durward M Radhakrishnan GK Brucella induces an unfolded protein response via TcpB that supports intracellular replication in macrophages. PLoS Pathog (2013) 9(12): e1003785. 10.1371/journal.ppat.1003785 24339776 PMC3855547 · DOI
  180. [183]Radhakrishnan GK Harms JS Splitter GA. Modulation of microtubule dynamics by a TIR domain protein from the intracellular pathogen Brucella melitensis. Biochem J (2011) 439(1): 79– 83. 10.1042/BJ20110577 21692747 PMC3513345 · DOI
  181. [184]Qin QM Pei J Ancona V Shaw BD Ficht TA de Figueiredo P. RNAi screen of endoplasmic reticulum-associated host factors reveals a role for IRE1alpha in supporting Brucella replication. PLoS Pathog (2008) 4(7): e1000110. 10.1371/journal.ppat.1000110 18654626 PMC2453327 · DOI
  182. [185]Deegan S Saveljeva S Gorman AM Samali A. Stress-induced self-cannibalism: on the regulation of autophagy by endoplasmic reticulum stress. Cell Mol Life Sci (2013) 70(14): 2425– 41. 10.1007/s00018-012-1173-4 23052213 PMC11113399 · DOI
  183. [186]Starr T Child R Wehrly TD Hansen B Hwang S López-Otin C Selective subversion of autophagy complexes facilitates completion of the Brucella intracellular cycle. Cell Host Microbe (2012) 11(1): 33– 45. 10.1016/j.chom.2011.12.002 22264511 PMC3266535 · DOI
  184. [187]Byndloss MX Tsolis RM. Brucella spp. Virulence factors and immunity. Annu Rev Anim Biosci (2016) 4: 111– 27. 10.1146/annurev-animal-021815-111326 26734887 · DOI
  185. [188]Radhakrishnan GK Yu Q Harms JS Splitter GA. Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRAP. J Biol Chem (2009) 284(15): 9892– 8. 10.1074/jbc.M805458200 19196716 PMC2665112 · DOI
  186. [189]Sag E Bilginer Y Ozen S. Autoinflammatory diseases with periodic fevers. Curr Rheumatol Rep (2017) 19(7): 41. 10.1007/s11926-017-0670-8 28631068 · DOI
  187. [190]Sherlock JP Joyce-Shaikh B Turner SP Chao CC Sathe M Grein J IL-23 induces spondyloarthropathy by acting on ROR-gammat+ CD3+CD4-CD8- entheseal resident T cells. Nat Med (2012) 18(7): 1069– 76. 10.1038/nm.2817 22772566 · DOI
  188. [191]Kontoyiannis D Pasparakis M Pizarro TT Cominelli F Kollias G. Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies. Immunity (1999) 10(3): 387– 98. 10.1016/S1074-7613(00)80038-2 10204494 · DOI
  189. [192]Hreggvidsdottir HS Noordenbos T Baeten DL. Inflammatory pathways in spondyloarthritis. Mol Immunol (2014) 57(1): 28– 37. 10.1016/j.molimm.2013.07.016 23969080 · DOI
  190. [193]Keffer J Probert L Cazlaris H Georgopoulos S Kaslaris E Kioussis D Transgenic mice expressing human tumour necrosis factor: a predictive genetic model of arthritis. EMBO J (1991) 10(13): 4025– 31. 1721867 PMC453150
  191. [194]Smith JA. Update on ankylosing spondylitis: current concepts in pathogenesis. Curr Allergy Asthma Rep (2015) 15(1): 489. 10.1007/s11882-014-0489-6 25447326 · DOI
  192. [195]Lees CW Barrett JC Parkes M Satsangi J. New IBD genetics: common pathways with other diseases. Gut (2011) 60(12): 1739– 53. 10.1136/gut.2009.199679 21300624 · DOI · Paper page
  193. [196]Ramos PS Criswell LA Moser KL Comeau ME Williams AH Pajewski NM A comprehensive analysis of shared loci between systemic lupus erythematosus (SLE) and sixteen autoimmune diseases reveals limited genetic overlap. PLoS Genet (2011) 7(12): e1002406. 10.1371/journal.pgen.1002406 22174698 PMC3234215 · DOI
  194. [198]Hugot JP Chamaillard M Zouali H Lesage S Cézard JP Belaiche J Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn’s disease. Nature (2001) 411(6837): 599– 603. 10.1038/35079107 11385576 · DOI · Paper page
  195. [199]Ogura Y Bonen DK Inohara N Nicolae DL Chen FF Ramos R A frameshift mutation in NOD2 associated with susceptibility to Crohn’s disease. Nature (2001) 411(6837): 603– 6. 10.1038/35079114 11385577 · DOI · Paper page
  196. [200]Kaser A Lee AH Franke A Glickman JN Zeissig S Tilg H XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell (2008) 134(5): 743– 56. 10.1016/j.cell.2008.07.021 18775308 PMC2586148 · DOI
  197. [201]Rioux JD Xavier RJ Taylor KD Silverberg MS Goyette P Huett A Genome-wide association study identifies new susceptibility loci for Crohn’s disease and implicates autophagy in disease pathogenesis. Nat Genet (2007) 39(5): 596– 604. 10.1038/ng2032 17435756 PMC2757939 · DOI · Paper page
  198. [202]Adolph TE Tomczak MF Niederreiter L Ko HJ Böck J Martinez-Naves E Paneth cells as a site of origin for intestinal inflammation. Nature (2013) 503(7475): 272– 6. 10.1038/nature12599 24089213 PMC3862182 · DOI · Paper page
  199. [203]Tschurtschenthaler M Adolph TE Ashcroft JW Niederreiter L Bharti R Saveljeva S Defective ATG16L1-mediated removal of IRE1alpha drives Crohn’s disease-like ileitis. J Exp Med (2017) 214(2): 401– 22. 10.1084/jem.20160791 28082357 PMC5294857 · DOI
  200. [204]Heazlewood CK Cook MC Eri R Price GR Tauro SB Taupin D Aberrant mucin assembly in mice causes endoplasmic reticulum stress and spontaneous inflammation resembling ulcerative colitis. PLoS Med (2008) 5(3): e54. 10.1371/journal.pmed.0050054 18318598 PMC2270292 · DOI · Paper page

200 of 279 shown

Cited by

Sorted by citations

Authors
Smith, J. A.
Affiliations
University of Wisconsin–Madison (US)
Corresponding author
Smith, Judith A.
ORCID
Smith, Judith A.
Venue
Frontiers in Immunology
Publisher
Frontiers Media SA
Published
2018-03-05
Volume
9
Pages
422-422
ISSN
1664-3224 (ISSN-L)
DOI
10.3389/fimmu.2018.00422
PMC
PMC5844972
OpenAlex
W2789523895
Cited by
168
References
6
Citations by year
2026: 8 · 2025: 20 · 2024: 21 · 2023: 13 · 2022: 32 · 2021: 24 · 2020: 25 · 2019: 21 · 2018: 4
FWCI
2.10
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Immunology (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institutes of Health (R01AI073558, R01 AI116453-01 and R21AI121808-01)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
unfolded protein response, endoplasmic reticulum stress, cytokine production, interferon, inflammatory cytokines, infection, autoimmunity, autoinflammatory disease, pattern recognition receptors, inflammatory signaling, viral infection, bacterial infection, HLA-B27, spondyloarthritis, autophagy, inflammatory bowel disease, diabetes mellitus
MeSH terms
Animals, Endoplasmic Reticulum, Humans, Infections, Inflammation, Spondylitis, Ankylosing, Inflammatory Bowel Diseases, Autoimmunity, Cytokines, Diabetes Complications, Receptors, Pattern Recognition, Unfolded Protein Response

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review