Abstract
Receptor-interacting protein kinases 1 and 3 (RIPK1 and RIPK3 ) are homologous serine–threonine kinases that were recognized for their roles in directing programmed necrotic cell death or necroptosis under a broad range of pathologic settings. Emerging evidence suggests new physiologic roles for RIPK1 and RIPK3 in mediating cell death of innate immune responses. Our review discusses current evidence on the mechanisms and the impact of RIPK1- and/or RIPK3-dependent cell death in responses to a variety of viral and bacterial pathogens. Furthermore, the discussion also summarizes emerging roles for RIPK1 and RIPK3 in other facets of host immunity, including the maintenance of epithelial barrier function and pro-inflammatory processes that may, in some cases, manifest independent of cell death. Finally, we briefly consider the therapeutic opportunities in targeting RIPK1- and RIPK3-dependent processes in infection and immunity.
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References
Albrecht ME (2014) Epidemiology, clinical manifestations, and diagnosis of genital herpes simplex virus infection. Uptodate http://www.uptodate.com/contents/epidemiology-clinical-manifestations-and-diagnosis-of-genital-herpes-simplex-virus-infection?source=search_result&search=HSV-2&selectedTitle=1~68
Alpuche-Aranda CM, Racoosin EL, Swanson JA, Miller SI (1994) Stimulate macrophage macropinocytosis and persist within spacious phagosomes. J Exp Med 179(2):601–608
Autheman D, Wyder M, Popoff M, D’Herde K, Christen S, Posthaus H (2013) Clostridium perfringens beta-toxin induces necrostatin-inhibitable, calpain-dependent necrosis in primary porcine endothelial cells. PloS One 8(5):e64644. doi:10.1371/journal.pone.0064644. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3667183&tool=pmcentrez&rendertype=abstract
Behnsen J, Perez-Lopez A, Nuccio SP, Raffatellu M (2015) Exploiting host immunity: the Salmonella paradigm. Trends Immunol 36(2):112–120. doi:10.1016/j.it.2014.12.003. http://linkinghub.elsevier.com/retrieve/pii/S1471490614002282
Berger AK, Danthi P (2013) Reovirus activates a caspase-independent cell death pathway. mBio 4(3):e00178–e001713. doi:10.1128/mBio.00178-13. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3656442&tool=pmcentrez&rendertype=abstract
Berger SB, Kasparcova V, Hoffman S, Swift B, Dare L, Schaeffer M, Capriotti C et al (2014) Cutting edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. J Immunol (Baltimore, Md. : 1950) (May 12). doi:10.4049/jimmunol.1400499. http://www.ncbi.nlm.nih.gov/pubmed/24821972
Bertin J, Armstron RC, Ottilie S, Martin DA, Wang Y, Banks S, Wang GH et al (1997) Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. Proc Natl Acad Sci 94(February):1172–1176
Best SM (2008) NIH public access pp 171–192. doi:10.1146/annurev.micro.62.081307.163009.Viral
Birnbaum MJ, Rollie JC, Lois KM (1994) An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs 68(4):2521–2528
Bischofberger M, Lacovache L, Gisou van der Goot F (2012) Pathogenic pore-forming proteins: function and host response. Cell Host Microbe 12(3):266–275. doi:10.1016/j.chom.2012.08.005. http://www.ncbi.nlm.nih.gov/pubmed/22980324
Bliska JB (2003) The ability to replicate in macrophages is conserved between yersinia pestis and Yersinia pseudotuberculosis 71(10):5892–5899. doi:10.1128/IAI.71.10.5892
Bonnet MC, Preukschat D, Welz PS, van Loo G, Ermolaeva MA, Bloch W, Haase I, Pasparakis M (2011) The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation. Immunity 35(4):572–582. doi:10.1016/j.immuni.2011.08.014. http://www.ncbi.nlm.nih.gov/pubmed/22000287
Boyden ED, Dietrich WF (2006) Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genetics 38(2):240–244. doi:10.1038/ng1724. http://www.ncbi.nlm.nih.gov/pubmed/16429160
Cai Z, Jitkaew S, Zhao J, Chiang HC, Choksi S, Liu J, Ward Y, Wu LG, Liu ZG (2014) Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biology 16(1):55–65. doi:10.1038/ncb2883. http://www.ncbi.nlm.nih.gov/pubmed/24316671
Cho Y, Challa S, Moquin D, Genga R, Dutta T, Guildford M, Chan MK (2010) NIH public access 137(6):1112–1123. doi:10.1016/j.cell.2009.05.037.Phosphorylation-Driven
Christofferson DE, Li Y, Hitomi J, Zhou W, Upperman C, Zhu H, Gerber SA, Gygi S, Yuan J (2012) A novel role for RIP1 kinase in mediating TNF-α production. Cell Death Dis 3:e320. doi:10.1038/cddis.2012.64. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3388236&tool=pmcentrez&rendertype=abstract
Christofferson DE, Li Y, Yuan J (2014) Control of life-or-death decisions by RIP1 kinase. Ann Rev Physiol 76:129–150. doi:10.1146/annurev-physiol-021113-170259. http://www.ncbi.nlm.nih.gov/pubmed/24079414
Christofferson DE, Yuan J (2010) Necroptosis as an alternative form of programmed cell death. Current Opinion Cell Biol 22(2):263–268. doi:10.1016/j.ceb.2009.12.003. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2854308&tool=pmcentrez&rendertype=abstract
Clarke P, Meintzer SM, Moffitt LA, Tyler KL (2003) Two distinct phases of virus-induced nuclear factor kappa B regulation enhance tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in virus-infected cells. J Biol Chem 278(20):18092–18100. doi:10.1074/jbc.M300265200. http://www.ncbi.nlm.nih.gov/pubmed/12637521
Craven RR, Gao X, Allen IC, Gris D, Bubeck Wardenburg J, McElvania-Tekippe E, Ting JP, Duncan JA (2009) Staphylococcus aureus alpha-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells. PloS One 4(10):e7446. doi:10.1371/journal.pone.0007446. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2758589&tool=pmcentrez&rendertype=abstract
Crook NE, Clem RJ, Miller LK (1993) An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif 67(4):2168–2174
Cuda CM, Misharin AV, Gierut AK, Saber R, Haines GK, Hutcheson J, Hedrick SM et al (2014) Caspase-8 acts as a molecular rheostat to limit RIPK1- and MyD88-mediated dendritic cell activation. J Immunol (Baltimore, Md. : 1950). doi:10.4049/jimmunol.1400122. http://www.ncbi.nlm.nih.gov/pubmed/24808358
Cusson-Hermance N, Khurana S, Lee TH, Fitzgerald KA, Kelliher MA (2005) Rip1 mediates the trif-dependent Toll-like receptor 3- and 4-induced NF-{kappa}B activation but does not contribute to interferon regulatory factor 3 activation. J Biol Chem 280(44):36560–36566. doi:10.1074/jbc.M506831200. http://www.ncbi.nlm.nih.gov/pubmed/16115877
Dannappel M, Vlantis K, Kumari S, Polykratis A, Kim C, Wachsmuth L, Eftychi C et al (2014) RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis. Nature 513(7516):90–94. doi:10.1038/nature13608. http://dx.doi.org/10.1038/nature13608
Danthi P, Holm GH, Stehle T, Dermody TS (2013) Chapter 3 Reovirus receptors, cell entry, and proapoptotic signaling pp 42–71
Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N, Cuny GD, Mitchison TJ, Moskowitz MA, Yuan J (2005) Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 1(2):112–119. doi:10.1038/nchembio711. http://www.ncbi.nlm.nih.gov/pubmed/16408008
Degterev A, Hitomi J, Germscheid M, Ch’en IL, Korkina O, Teng X, Abbott D et al (2008) Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat Chem Biol 4(5):313–321. doi:10.1038/nchembio.83. http://www.ncbi.nlm.nih.gov/pubmed/18408713
Degterev A, Maki JL, Yuan J (2013) Activity and specificity of necrostatin-1, small-molecule inhibitor of RIP1 kinase. Cell Death Differ 20(2):366. doi:10.1038/cdd.2012.133. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3554332&tool=pmcentrez&rendertype=abstract
Demmler-Harrison GJ (2015) Congenital cytomegalovirus infection: clinical features and diagnosis. Uptodate. http://www.uptodate.com/contents/congenital-cytomegalovirus-infection-clinical-features-and-diagnosis?source=search_result&search=cmv&selectedTitle=2~150
Deveraux QL, Reed JC (1999) REVIEW IAP family proteins—suppressors of apoptosis, pp 239–252
Dillon CP, Weinlich R, Rodriguez DA, Cripps JG, Quarato G, Gurung P, Verbist KC et al (2014) RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3. Cell 157(5):1189–1202. doi:10.1016/j.cell.2014.04.018. http://www.ncbi.nlm.nih.gov/pubmed/24813850
Goldstein DJ, Weller SK (1988) Factor(s) present in herpes simplex virus type 1-infected cells can compensate for the loss of the large subunit of the viral ribonucleotide reductase: characterization of an ICP6 deletion mutant. Virology 166(1):41–51
Dobbelstein M, Shenk T, Hughes H (1996) Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product. Mol Biol 70(9):6479–6485
Dolin R (2015) Epidemiology of influenza. Uptodate. http://www.uptodate.com/contents/epidemiology-of-influenza?source=search_result&search=Dolin+INfluenza&selectedTitle=3~150
Dondelinger Y, Aguileta MA, Goossens V, Dubuisson C, Grootjans S, Dejardin E, Vandenabeele P, Bertrand MJM (2013) RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ 20(10):1381–1392. doi:10.1038/cdd.2013.94. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3770330&tool=pmcentrez&rendertype=abstract
Dufour F, Sasseville A, Chabaud S, Massie B, Siegel RM, Langelier Y (2011) The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNF-α- and FasL-Induced apoptosis by interacting with caspase-8. Apoptosis Int J Programmed Cell Death 16(3):256–271. doi:10.1007/s10495-010-0560-2. http://www.ncbi.nlm.nih.gov/pubmed/21107701
Elias PM (2007) The skin barrier as an innate immune element. Semin Immunopathol 3(14):3–14
Faherty CS, Maurelli AT (2008) Staying alive: bacterial inhibition of apoptosis during infection. Trends Microbiol 16(4):173–180. doi:10.1016/j.tim.2008.02.001. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2746948&tool=pmcentrez&rendertype=abstract
Friel TJ (2014) Epidemiology, clinical manifestations, and treatment of cytomegalovirus infection in immunocompetent adults. Uptodate. http://www.uptodate.com/contents/epidemiology-clinical-manifestations-and-treatment-of-cytomegalovirus-infection-in-immunocompetent-adults?source=search_result&search=cmv&selectedTitle=1~150
Galluzzi L, Kepp O, Morselli E, Vitale I, Senovilla L, Pinti M, Zitvogel L, Kroemer G (2010) Viral strategies for the evasion of immunogenic cell death. J Intern Med 267(5):526–542. doi:10.1111/j.1365-2796.2010.02223.x. http://www.ncbi.nlm.nih.gov/pubmed/20433579
Günther C, Martini E, Wittkopf N, Amann K, Weigmann B, Neumann H, Waldner MJ et al (2011) Caspase-8 regulates TNF-Α-induced epithelial necroptosis and terminal Ileitis. Nature 477(7364):335–339. doi:10.1038/nature10400. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3373730&tool=pmcentrez&rendertype=abstract
Guo W, Allan AM, Zong R, Zhang L, Johnson EB, Schaller EG, Murthy AC et al (2011) Ablation of Fmrp in adult neural stem cells disrupts hippocampus-dependent learning. Nat Med 17(5):559–565. doi:10.1038/nm.2336. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3140952&tool=pmcentrez&rendertype=abstract
Guo H, Omoto S, Harris PA, Finger JN, Bertin J, Gough PJ, Kaiser WJ, Mocarski ES (2015) Herpes simplex virus suppresses necroptosis in human cells. Cell Host Microbe 17(2):243–251. doi:10.1016/j.chom.2015.01.003. http://www.ncbi.nlm.nih.gov/pubmed/25674983
He S, Wang L, Miao L, Wang T, Du F, Zhao L, Wang X (2009) Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 137(6):1100–1111. doi:10.1016/j.cell.2009.05.021. http://www.ncbi.nlm.nih.gov/pubmed/19524512
Hildebrand JM, Tanzer MC, Lucet IS, Young SN, Spall SK, Sharma P, Pierotti C et al (2014) Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death. Proc Nat Acad Sci USA 111(42). doi:10.1073/pnas.1408987111. http://www.ncbi.nlm.nih.gov/pubmed/25288762
Hitomi J, Christofferson DE, Ng A, Yao J, Degterev A, Xavier RJ, Yuan J (2008) Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 135(7):1311–1323. doi:10.1016/j.cell.2008.10.044. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2621059&tool=pmcentrez&rendertype=abstract
Hohmann EL (2014) Microbiology and epidemiology of salmonellosis. Uptodate. http://www.uptodate.com/contents/microbiology-and-epidemiology-of-salmonellosis?source=search_result&search=Salmonella&selectedTitle=2~150
Hu S, Vincenz C, Buller M, Dixit VM (1997) A novel family of viral death effector domain-containing molecules that inhibit both C-95 an tumor necrosis factor receptor-1-induced apoptosis *. J Biol Chem 272(15):9621–9625
Huang Z, Wu SQ, Liang Y, Zhou X, Chen W, Li L, Wu J et al (2015) RIP1/RIP3 binding to HSV-1 ICP6 initiates necroptosis to restrict virus propagation in mice. Cell Host Microbe 17(2):229–242. doi:10.1016/j.chom.2015.01.002. http://www.ncbi.nlm.nih.gov/pubmed/25674982
Kabsch K, Alonso A (2002) The human papillomavirus type 16 E5 protein impairs TRAIL- and FasL-mediated apoptosis in HaCaT cells by different mechanisms. J Virol 76(23):12162–12172. doi:10.1128/JVI.76.23.12162-12172.2002. http://jvi.asm.org/cgi/doi/10.1128/JVI.76.23.12162-12172.2002
Kaczmarek A, Vandenabeele P, Krysko DV (2013) Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity 38(2):209–223. doi:10.1016/j.immuni.2013.02.003. http://www.ncbi.nlm.nih.gov/pubmed/23438821
Kaiser WJ, Sridharan H, Huang C, Mandal P, Upton JW, Gough PJ, Sehon CA, Marquis RW, Bertin J, Mocarski ES (2013) Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL. J Biol Chem 288(43):31268–31279. doi:10.1074/jbc.M113.462341. http://www.ncbi.nlm.nih.gov/pubmed/24019532
Kaiser WJ, Daley-Bauer LP, Thapa RJ, Mandal P, Berger SB, Huang C, Sundararajan A et al (2014) RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc Nat Acad Sci USA 111(21):7753–7758. doi:10.1073/pnas.1401857111. http://www.ncbi.nlm.nih.gov/pubmed/24821786
Kang TB, Yang SH, Toth B, Kovalenko A, Wallach D (2014) Activation of the NLRP3 inflammasome by proteins that signal for necroptosis. Methods Enzymol, 1st ed, vol 545. Elsevier Inc. doi:10.1016/B978-0-12-801430-1.00003-2. http://www.ncbi.nlm.nih.gov/pubmed/25065886
Kaser A, Zeissig S, Blumberg RS (2010) Inflammatory bowel disease. Ann Rev Immunol 28:573–621. doi:10.1146/annurev-immunol-030409-101225. http://www.ncbi.nlm.nih.gov/pubmed/20192811
Kearney CJ, Cullen SP, Clancy D, Martin SJ (2014) RIPK1 can function as an inhibitor rather than an initiator of RIPK3-dependent necroptosis. FEBS J. doi:10.1111/febs.13034. http://www.ncbi.nlm.nih.gov/pubmed/25195660
Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P (1998) The death domain kinase RIP mediates the TNF-induced NF—B signal 8:297–303
Kennedy CL, Smith DJ, Lyras D, Chakravorty A, Rood JI (2009) Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum. PLoS Pathogens 5(7):e1000516. doi:10.1371/journal.ppat.1000516. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2705182&tool=pmcentrez&rendertype=abstract
Kim SJ, Jianrong Li (2013) Caspase blockade induces RIP3-mediated programmed necrosis in Toll-like receptor-activated microglia. Cell Death Dis 4(7):e716. doi:10.1038/cddis.2013.238. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3730412&tool=pmcentrez&rendertype=abstract
Kitur K, Parker D, Nieto P, Ahn DS, Cohen TS, Chung S, Wachtel S, Bueno S, Prince A (2015) Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage. PLoS Pathogens 11(4):e1004820. doi:10.1371/journal.ppat.1004820. http://www.ncbi.nlm.nih.gov/pubmed/25880560
Klein RS (2015a) Clinical manifestations and diagnosis of herpes simplex virus type 1 infection. Uptodate http://www.uptodate.com/contents/clinical-manifestations-and-diagnosis-of-herpes-simplex-virus-type-1-infection?source=search_result&search=HSV&selectedTitle=1~150
Klein RS (2015b) Herpes simplex virus type 1 encephalitis. Uptodate http://www.uptodate.com/contents/herpes-simplex-virus-type-1-encephalitis?source=search_result&search=HSV+encephalitis&selectedTitle=1~46
Knapp O, Maier E, Mkaddem SB, Benz R, Bens M, Chenal A, Geny B, Vandewalle A, Popoff MR (2010) Clostridium septicum alpha-toxin forms pores and induces rapid cell necrosis. Toxicon Official J Int Soc Toxinol 55(1):61–72. doi:10.1016/j.toxicon.2009.06.037. http://www.ncbi.nlm.nih.gov/pubmed/19632260
Kotton CN, Hohmann EL (2013) Pathogenesis of salmonella gastroenteritis. Uptodate http://www.uptodate.com/contents/pathogenesis-of-salmonella-gastroenteritis?source=search_result&search=Salmonella&selectedTitle=3~150
Kovalenko A, Kim JC, Kang TB, Rajput A, Bogdanov K, Dittrich-Breiholz O, Kracht M, Brenner O, Wallach D (2009) Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease. J Exp Med 206(10):2161–2177. doi:10.1084/jem.20090616. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2757876&tool=pmcentrez&rendertype=abstract
Kumar V, Abul AK, Fausto N, Aster J (2010) Pathologic basis of disease, 8th ed. Saunders
Lamkanfi M, Dixit VM (2010) Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 8(1):44–54. doi:10.1016/j.chom.2010.06.007. http://www.ncbi.nlm.nih.gov/pubmed/20638641
Langelier Y, Bergeron S, Chabaud S, Lippens J, Guilbault C, Sasseville AM, Denis S, Mosser DD, Massie B (2002) The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation, pp 2779–2789
LaRock CN, Cookson BT (2012) The yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing. Cell Host Microbe 12(6):799–805. doi:10.1016/j.chom.2012.10.020. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3703949&tool=pmcentrez&rendertype=abstract
Li M, Beg AA (2000) Induction of necrotic-like cell death by tumor necrosis factor alpha and caspase inhibitors : novel mechanism for killing virus-infected cells 74(16):7470–7477
Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E et al (2012) The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150(2):339–350. doi:10.1016/j.cell.2012.06.019. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3664196&tool=pmcentrez&rendertype=abstract
Li S, Zhang L, Yao Q, Li L, Dong N, Rong J, Gao W et al (2013) Pathogen blocks host death-receptor signalling by arginine GlcNAcylation of death domains. Nature 501(7466):242–246. doi:10.1038/nature12436. http://www.ncbi.nlm.nih.gov/pubmed/23955153
Li L, Chen W, Liang Y, Ma H, Li W, Zhou Z, Li J et al (2014) The Gβγ-src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocation. Cell Res 2:1–16. doi:10.1038/cr.2014.17. http://www.ncbi.nlm.nih.gov/pubmed/24513853
Lin CF, Chen CL, Huang WC, Cheng YL, Hsieh CY, Wang CY, Hong MY (2010) Different types of cell death induced by enterotoxins. Toxins 2(8):2158–2176. doi:10.3390/toxins2082158. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3153280&tool=pmcentrez&rendertype=abstract
Linkermann A, Green DR (2014) Necroptosis. New Engl J Med 370(5):455–465. doi:10.1056/NEJMra1310050. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4035222&tool=pmcentrez&rendertype=abstract
Lukens JR, Vogel P, Johnson GR, Kelliher MA, Iwakura Y, Lamkanfi M, Kanneganti TD (2013) RIP1-driven autoinflammation targets IL-1α independently of inflammasomes and RIP3. Nature 498(7453):224–227. doi:10.1038/nature12174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3683390&tool=pmcentrez&rendertype=abstract
Macdonald TT, Monteleone G (2005) Immunity, inflammation, and allergy in the gut pp 1920–1925
Macen JL, Garner RS, Musyt PY, Brookst MA, Turnert PC, Moyert RW, Mcfadden G, Bleackley RC (1996) Orthopoxvirus cytokine 93:9108–9113
McComb S, Cheung HH, Korneluk RG, Wang S, Krishnan L, Sad S (2012) cIAP1 and cIAP2 limit macrophage necroptosis by inhibiting Rip1 and Rip3 activation. Cell Death Differ 19(11):1791–1801. doi:10.1038/cdd.2012.59. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3469059&tool=pmcentrez&rendertype=abstract
McCoy MW, Moreland SM, Detweiler CS (2012) Hemophagocytic macrophages in murine typhoid fever have an anti-inflammatory phenotype. Infect Immun 80(10):3642–3649. doi:10.1128/IAI.00656-12. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3457584&tool=pmcentrez&rendertype=abstract
Meylan E, Burns K, Hofmann K, Blancheteau V, Martinon F, Kelliher M, Tschopp J (2004) RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation. Nat Immunol 5(5):503–507. doi:10.1038/ni1061. http://www.ncbi.nlm.nih.gov/pubmed/15064760
Miller EA, Ernst JD (2009) Anti-TNF immunotherapy and tuberculosis reactivation: another mechanism revealed. J Clin Invest 119(5):1079–1082. doi:10.1172/JCI39143. http://www.jci.org/articles/view/39143
Mocarski ES, Upton JW, Kaiser WJ (2012) Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways. Nat Rev Immunol 12(2):79–88. doi:10.1038/nri3131. http://www.ncbi.nlm.nih.gov/pubmed/22193709
Moquin DM, McQuade T, Chan FK (2013) CYLD deubiquitinates RIP1 in the TNF-α-induced necrosome to facilitate kinase activation and programmed necrosis. PloS One 8(10):e76841. doi:10.1371/journal.pone.0076841. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3788787&tool=pmcentrez&rendertype=abstract
Moriwaki K, Balaji S, McQuade T, Malhotra N, Kang J, Chan FK (2014) The necroptosis adaptor RIPK3 promotes injury-induced cytokine expression and tissue repair. Immunity 41(4):567–578. doi:10.1016/j.immuni.2014.09.016. http://linkinghub.elsevier.com/retrieve/pii/S1074761314003501
Moriwaki K, Bertin J, Gough PJ, Chan FK (2015) A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing. J Immunol (Baltimore, Md. : 1950) 194(4):1938–1944. doi:10.4049/jimmunol.1402167. http://www.ncbi.nlm.nih.gov/pubmed/25567679
Murphy JM, Czabotar PE, Hildebrand JM, Lucet IS, ZhangJG, Alvarez-Diaz S, Lewis R et al (2013) The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39(3):443–453. doi:10.1016/j.immuni.2013.06.018. http://www.ncbi.nlm.nih.gov/pubmed/24012422
Nestle FO, Meglio PD, Qin JZ, Nickoloff BJ (2009) Skin immune sentinels in health and disease. Nat Rev Immunol 9(10):679–691. doi:10.1038/nri2622. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2947825&tool=pmcentrez&rendertype=abstract
Nix RN, Altschuler SE, Henson PM, Detweiler CS (2007) Hemophagocytic macrophages harbor salmonella enterica during persistent infection. PLoS Pathog 3(12):e193. doi:10.1371/journal.ppat.0030193. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2134957&tool=pmcentrez&rendertype=abstract
O’Ryan MG., Matson DO (2015) Clinical manifestations and diagnosis of rotavirus infection. Uptodate http://www.uptodate.com/contents/clinical-manifestations-and-diagnosis-of-rotavirus-infection?source=search_result&search=rotavirus&selectedTitle=1~82
Ofengeim D, Yuan J (2013) Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death. Nat Rev Mol Cell Biol 14(11):727–736. doi:10.1038/nrm3683. http://www.ncbi.nlm.nih.gov/pubmed/24129419
Ofengeim D, Ito Y, Najafov A, Zhang Y, Shan B, DeWitt JP, Ye J et al (2015) Activation of necroptosis in multiple sclerosis. Cell Rep 10(11):1836–1849. doi:10.1016/j.celrep.2015.02.051. http://www.ncbi.nlm.nih.gov/pubmed/25801023
Omoto S, Guo H, Talekar GR, Roback L, Kaiser WJ, Mocarski E (2015) Suppression of RIP3-dependent necroptosis by human cytomegalovirus. J Biol Chem (404). doi:10.1074/jbc.M115.646042. http://www.ncbi.nlm.nih.gov/pubmed/25778401
Orozco S, Yatim N, Werner MR, Tran H, Gunja SY, Wg Tait S, Albert ML, Green DR, Oberst A (2014) RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis. Cell Death Differ 21(10):1511–1521. doi:10.1038/cdd.2014.76. http://www.ncbi.nlm.nih.gov/pubmed/24902904
Osborn SL, Diehl G, Han SJ, Xue L, Kurd N, Hsieh K, Cado D, Robey EA, Winoto A (2010) Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis. Proc Nat Acad Sci USA 107(29):13034–13039. doi:10.1073/pnas.1005997107. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2919948&tool=pmcentrez&rendertype=abstract
Pearson JS, Giogha C, Ong SY, Kennedy CL, Kelly M, Robinson KS, Fok Lung TW et al (2013) A type III effector antagonizes death-receptor signalling during bacterial gut infection. Nature 501(7466):247–251. doi:10.1038/nature12524. http://www.nature.com/doifinder/10.1038/nature12524
Philip NH, Dillon CP, Snyder AG, Fitzgerald P, Wynosky-Dolfi MA, Zwack EE, Hu B et al (2014) Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-κB and MAPK signaling. Proc Nat Acad Sci USA 111(20):7385–7390. doi:10.1073/pnas.1403252111. http://www.ncbi.nlm.nih.gov/pubmed/24799700
Polykratis A, Hermance N, Zelic M, Roderick J, Kim C, Van TM, Lee TH, Chan FKM, Pasparakis M, Kelliher MA (2014) Cutting edge: RIPK1 kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo. J Immunol (Baltimore, Md. : 1950). doi:10.4049/jimmunol.1400590. http://www.ncbi.nlm.nih.gov/pubmed/25015821
Pozniak A (2015) Clinical manifestations and evaluation of pulmonary tuberculosis. Uptodate http://www.uptodate.com/contents/clinical-manifestations-and-evaluation-of-pulmonary-tuberculosis?source=search_result&search=Clinical+manifestations+and+evaluation+of+pulmonary+tb&selectedTitle=1~107
Pujol C, Bliska JB (2003) The ability to replicate in macrophages is conserved between yersinia pestis and yersinia pseudotuberculosis. Infect Immun 71(10):5892–5899. doi:10.1128/IAI.71.10.5892-5899.2003. http://iai.asm.org/cgi/doi/10.1128/IAI.71.10.5892-5899.2003
Pujol C, Bliska JB (2005) Turning yersinia pathogenesis outside in: subversion of macrophage function by intracellular yersiniae. Clin Immunol (Orlando, Fla.) 114(3):216–226. doi:10.1016/j.clim.2004.07.013. http://www.ncbi.nlm.nih.gov/pubmed/15721832
Pujol C, Klein KA, Romanov GA, Palmer LE, Cirota C, Zhao Z, Bliska JB (2009) Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification. Infect Immun 77(6):2251–2261. doi:10.1128/IAI.00068-09. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2687347&tool=pmcentrez&rendertype=abstract
Rajput A, Kovalenko A, Bogdanov K, Yang SH, Kang TB, Kim JC, Du J, Wallach D (2011) RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein. Immunity 34(3):340–351. doi:10.1016/j.immuni.2010.12.018. http://www.ncbi.nlm.nih.gov/pubmed/21419663
Richardson-Burns SM, Kominsky DJ, Tyler KL (2002) Reovirus-induced neuronal apoptosis is mediated by caspase 3 and is associated with the activation of death-receptors, pp 365–380. doi:10.1080/13550280290100806
Rickard JA, O’Donnell JA, Evans JM, Lalaoui N, Poh AR, Rogers T, Vince JE et al (2014) RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell 8:1–14. doi:10.1016/j.cell.2014.04.019. http://www.ncbi.nlm.nih.gov/pubmed/24813849
Robinson N, McComb S, Mulligan R, Dudani R, Krishnan L, Sad S (2012) Type i interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar typhimurium. Nat Immunol 13(10):954–962. doi:10.1038/ni.2397. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4005791&tool=pmcentrez&rendertype=abstract
Roca FJ, Ramakrishnan L (2013) TNF dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species. Cell 153(3):521–534. doi:10.1016/j.cell.2013.03.022. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3790588&tool=pmcentrez&rendertype=abstract
Rodrigue-Gervais IG, Labbé K, Dagenais M, Dupaul-Chicoine J, Champagne C, Morizot A, Skeldon A et al (2014) Cellular inhibitor of apoptosis protein cIAP2 protects against pulmonary tissue necrosis during influenza virus infection to promote host survival. Cell Host Microbe 15(1):23–35. doi:10.1016/j.chom.2013.12.003. http://www.ncbi.nlm.nih.gov/pubmed/24439895
Roy CR, Mocarski ES (2007) Pathogen subversion of cell-intrinsic innate immunity. Nat Immunol 8(11):1179–1187. doi:10.1038/ni1528. http://www.ncbi.nlm.nih.gov/pubmed/17952043
Schluger NW, Rom WN (1998) The host immune response to tuberculosis. Am J Respir Crit Care Med 157(19). Retrieved from http://www.atsjournals.org/doi/abs/10.1164/ajrccm.157.3.9708002
Sexton DJ (2014) Epidemiology, microbiology and pathogenesis of plague (yersinia pestis infection). Uptodate http://www.uptodate.com/contents/epidemiology-microbiology-and-pathogenesis-of-plague-yersinia-pestis-infection?source=search_result&search=Pestis&selectedTitle=1~25
Shisler JL, Moss B (2001) Molluscum contagiosum virus inhibitors of apoptosis: the MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein. Virology 282(1):14–25. doi:10.1006/viro.2001.0834. http://www.ncbi.nlm.nih.gov/pubmed/11259186
Skaletskaya A, Bartle LM, Chittenden T, McCormick AL, Mocarski ES, Goldmacher VS (2001) A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation. Proc Nat Acad Sci USA 98(14):7829–7834. doi:10.1073/pnas.141108798. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=35427&tool=pmcentrez&rendertype=abstract
Sridharan H, Upton JW (2014) Programmed necrosis in microbial pathogenesis. Trends Microbiol 22(4):199–1207. doi:10.1016/j.tim.2014.01.005. http://www.ncbi.nlm.nih.gov/pubmed/24565922
Takahashi N, Vereecke L, Bertrand MJ, Duprez L, Berger SB, Divert T, Gonçalves A et al (2014) RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis. Nature 513(7516):95–99. doi:10.1038/nature13706. http://www.nature.com/doifinder/10.1038/nature13706
Tauxe RV (2013) Clinical manifestations and diagnosis of yersinia infections. Uptodate http://www.uptodate.com/contents/clinical-manifestations-and-diagnosis-of-yersinia-infections?source=search_result&search=Yersinia&selectedTitle=1~92
Thome M, Schneider P, Hofman K, Ficjenscher H, Meini E, Neipel F, Mattmann C et al (1997) Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death-receptors.pdf. Nature 386:517–521
Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M (2006) The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. Cell Death Differ 13(9):1577–1585. doi:10.1038/sj.cdd.4401847. http://www.ncbi.nlm.nih.gov/pubmed/16410799
Ting AT, Pimentel-Muiffios FX (1996) RIP activation apoptosis 15(22):6189–6196
Tobin DM, Vary JC, Ray JP, Walsh GS, Dunstan SJ, Bang ND, Hagge DA et al (2010) The lta4 h locus modulates susceptibility to mycobacterial infection in zebrafish and humans. Cell 140(5):717–730. doi:10.1016/j.cell.2010.02.013. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2907082&tool=pmcentrez&rendertype=abstract
Tobin DM, Roca FJ, Oh SF, McFarland R, Vickery TW, Ray JP, Ko DC et al (2012) Host genotype-specific therapies can optimize the inflammatory response to mycobacterial infections. Cell 148(3):434–446. doi:10.1016/j.cell.2011.12.023. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3433720&tool=pmcentrez&rendertype=abstract
Turner SJ, Silke J, Kenshole B, Ruby J (2000) Characterization of the ectromelia virus serpin, SPI-2 64:2425–2430
Ulrichs T, Kaufmann SHE (2006) New insights into the function of granulomas in human tuberculosis. J Pathol 208(2):261–269. doi:10.1002/path.1906. http://www.ncbi.nlm.nih.gov/pubmed/16362982
Upton JW, Kaiser WJ, Mocarski ES (2010) Virus inhibition of RIP3-dependent necrosis. Cell Host Microbe 7(4):302–313. doi:10.1016/j.chom.2010.03.006. http://www.ncbi.nlm.nih.gov/pubmed/20413098
Upton JW, Kaiser WJ, Mocarski ES (2012) DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA. Cell Host Microbe 11(3):290–297. doi:10.1016/j.chom.2012.01.016. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3531981&tool=pmcentrez&rendertype=abstract
Vanden Berghe T, Linkermann A, Jouan-Lanhouet S, Walczak H, Vandenabeele P (2014) Regulated necrosis: the expanding network of non-apoptotic cell death pathways. Nat Rev Mol Cell Biol 15(2):135–147. doi:10.1038/nrm3737. http://www.ncbi.nlm.nih.gov/pubmed/24452471
Vandenabeele P, Declercq W, Van Herreweghe F, Berghe TV (2010a) The role of the kinases RIP1 and RIP3 in TNF-induced necrosis. Sci Signaling 3(115):re4. doi:10.1126/scisignal.3115re4. http://www.ncbi.nlm.nih.gov/pubmed/20354226
Vandenabeele P, Galluzzi L, Berghe TV, Kroemer G (2010b) Molecular mechanisms of necroptosis: an ordered cellular explosion. Nat Rev Mol Cell Biol 11(10):700–714. doi:10.1038/nrm2970. http://www.ncbi.nlm.nih.gov/pubmed/20823910
Viboud GI, Bliska JB (2005) Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Ann Rev Microbiol 59:69–89. doi:10.1146/annurev.micro.59.030804.121320. http://www.ncbi.nlm.nih.gov/pubmed/15847602
Wang X, Jiang W, Yan Y, Gong T, Han J, Tian Z, Zhou R (2014a) RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway. Nat Immunol 15(12). doi:10.1038/ni.3015. http://www.nature.com/doifinder/10.1038/ni.3015
Wang X, Li Y, Liu S, Yu X, Li L, Shi C, He W et al (2014b) Direct activation of RIP3/MLKL-dependent necrosis by herpes simplex virus 1 (HSV-1) protein ICP6 triggers host antiviral defense. Proc Nat Acad Sci USA 111(43):15438–15443. doi:10.1073/pnas.1412767111. http://www.ncbi.nlm.nih.gov/pubmed/25316792
Wanke CA (2013) Pathogenic Escherichia coli. Uptodate http://www.uptodate.com/contents/pathogenic-escherichia-coli?source=search_result&search=E.coli&selectedTitle=1~150
Weinlich R, Oberst A, Dillon CP, Janke LJ, Milasta S, Lukens JR, Rodriguez DA et al (2013) Protective roles for caspase-8 and cFLIP in adult homeostasis. Cell Reports 5(2):340–348. doi:10.1016/j.celrep.2013.08.045. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3843376&tool=pmcentrez&rendertype=abstract
Welz PS, Wullaert A, Vlantis K, Kondylis V, Fernández-Majada V, Ermolaeva M, Kirsch P, Sterner-Kock A, van Loo G, Pasparakis M (2011) FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation. Nature 477(7364):330–334. doi:10.1038/nature10273. http://www.ncbi.nlm.nih.gov/pubmed/21804564
Weng D, Marty-Roix R, Ganesan S, Proulx MK, Vladimer GI, Kaiser WJ, Mocarski ES, et al (2014) Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death. Proc Nat Acad Sci USA 111(20):7391–7396. doi:10.1073/pnas.1403477111. http://www.ncbi.nlm.nih.gov/pubmed/24799678
Wu J, Huang Z, Ren J, Zhang Z, He P, Li Y, Ma J et al (2013) Mlkl knockout mice demonstrate the indispensable role of mlkl in necroptosis. Cell Res 23(8):994–1006. doi:10.1038/cr.2013.91. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3731568&tool=pmcentrez&rendertype=abstract
Wu XN, Yang ZH, Wang XK, Zhang Y, Wan H, Song Y, Chen X, Shao J, Han J (2014) Distinct roles of RIP1-RIP3 hetero- and RIP3-RIP3 homo-interaction in mediating necroptosis. Cell Death Differ 1–12. doi:10.1038/cdd.2014.77. http://www.ncbi.nlm.nih.gov/pubmed/24902902
Xie T, Peng W, Liu Y, Yan C, Maki J, Degterev A, Yuan J, Shi Y (2013a) Structural basis of RIP1 inhibition by necrostatins. Structure (London, England : 1993) 21(3):493–499. doi:10.1016/j.str.2013.01.016. http://www.ncbi.nlm.nih.gov/pubmed/23473668
Xie T, Peng W, Yan C, Wu J, Gong X, Shi Y (2013b) Structural insights into RIP3-mediated necroptotic signaling. Cell Rep 5(1):70–78. doi:10.1016/j.celrep.2013.08.044. http://www.ncbi.nlm.nih.gov/pubmed/24095729
Yatim N, Albert ML (2011) Dying to replicate: the orchestration of the viral life cycle, cell death pathways, and immunity. Immunity 35(4):478–490. doi:10.1016/j.immuni.2011.10.010. http://www.ncbi.nlm.nih.gov/pubmed/22035840
You Z, Savitz SI, Yang J, Degterev A, Yuan J, Cuny GD, Moskowitz MA, WhalenMJ (2008) Necrostatin-1 reduces histopathology and improves functional outcome after controlled cortical impact in mice. J Cereb Blood Flow Metab Official J Int Soc Cereb Blood Flow Metab 28(9):1564–1573. doi:10.1038/jcbfm.2008.44. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2831087&tool=pmcentrez&rendertype=abstract
Zhang SQ, Kovalenko A, Cantarella G, Wallach D (2000) Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation 12:301–311
Zhang DW, Shao J, Lin J, Zhang N, Lu BL, Lin SC, Dong MQ, Han J (2009) RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science (New York) 325(5938):332–336. doi:10.1126/science.1172308. http://www.ncbi.nlm.nih.gov/pubmed/19498109
Zhang Y, Romanov G, Bliska JB (2011) Type III secretion system-dependent translocation of ectopically expressed yop effectors into macrophages by intracellular yersinia pseudotuberculosis. Infect Immun 79(11):4322–4331. doi:10.1128/IAI.05396-11. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3257923&tool=pmcentrez&rendertype=abstract
Zhao J, Jitkaew S, Cai Z, Choksi S, Li Q, Luo J, Liu ZG (2012) Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Nat Acad Sci USA 109(14):5322–5327. doi:10.1073/pnas.1200012109. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3325682&tool=pmcentrez&rendertype=abstract
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Saleh, D., Degterev, A. (2015). Emerging Roles for RIPK1 and RIPK3 in Pathogen-Induced Cell Death and Host Immunity. In: Nagata, S., Nakano, H. (eds) Apoptotic and Non-apoptotic Cell Death. Current Topics in Microbiology and Immunology, vol 403. Springer, Cham. https://doi.org/10.1007/82_2015_449
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