메뉴 건너뛰기




Volumn 5, Issue 1, 2009, Pages 72-83

Virus-Induced Unfolded Protein Response Attenuates Antiviral Defenses via Phosphorylation-Dependent Degradation of the Type I Interferon Receptor

Author keywords

CELLBIO; MICROBIO; MOLIMMUNO

Indexed keywords

INTERFERON RECEPTOR; INTERFERON RECEPTOR 1; PROTEIN KINASE; PROTEIN PERK; UNCLASSIFIED DRUG;

EID: 58249084172     PISSN: 19313128     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chom.2008.11.008     Document Type: Article
Times cited : (116)

References (54)
  • 1
    • 8644224931 scopus 로고    scopus 로고
    • Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR
    • Baltzis D., Qu L.K., Papadopoulou S., Blais J.D., Bell J.C., Sonenberg N., and Koromilas A.E. Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR. J. Virol. 78 (2004) 12747-12761
    • (2004) J. Virol. , vol.78 , pp. 12747-12761
    • Baltzis, D.1    Qu, L.K.2    Papadopoulou, S.3    Blais, J.D.4    Bell, J.C.5    Sonenberg, N.6    Koromilas, A.E.7
  • 3
    • 0034954034 scopus 로고    scopus 로고
    • Interferons alpha and beta as immune regulators-a new look
    • Biron C.A. Interferons alpha and beta as immune regulators-a new look. Immunity 14 (2001) 661-664
    • (2001) Immunity , vol.14 , pp. 661-664
    • Biron, C.A.1
  • 4
    • 0018350377 scopus 로고
    • Mechanisms of interferon induced transfer of viral resistance between animal cells
    • Blalock J.E., and Baron S. Mechanisms of interferon induced transfer of viral resistance between animal cells. J. Gen. Virol. 42 (1979) 363-372
    • (1979) J. Gen. Virol. , vol.42 , pp. 363-372
    • Blalock, J.E.1    Baron, S.2
  • 5
    • 0036554140 scopus 로고    scopus 로고
    • Interferon-alpha as an immunotherapeutic protein
    • Brassard D.L., Grace M.J., and Bordens R.W. Interferon-alpha as an immunotherapeutic protein. J. Leukoc. Biol. 71 (2002) 565-581
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 565-581
    • Brassard, D.L.1    Grace, M.J.2    Bordens, R.W.3
  • 6
    • 0037100434 scopus 로고    scopus 로고
    • IFN-beta pretreatment sensitizes human melanoma cells to TRAIL/Apo2 ligand-induced apoptosis
    • Chawla-Sarkar M., Leaman D.W., Jacobs B.S., and Borden E.C. IFN-beta pretreatment sensitizes human melanoma cells to TRAIL/Apo2 ligand-induced apoptosis. J. Immunol. 169 (2002) 847-855
    • (2002) J. Immunol. , vol.169 , pp. 847-855
    • Chawla-Sarkar, M.1    Leaman, D.W.2    Jacobs, B.S.3    Borden, E.C.4
  • 7
    • 0036016562 scopus 로고    scopus 로고
    • Resistance to interferons in melanoma cells does not correlate with the expression or activation of signal transducer and activator of transcription 1 (stat1)
    • Chawla-Sarkar M., Leaman D.W., Jacobs B.S., Tuthill R.J., Chatterjee-Kishore M., Stark G.R., and Borden E.C. Resistance to interferons in melanoma cells does not correlate with the expression or activation of signal transducer and activator of transcription 1 (stat1). J. Interferon Cytokine Res. 22 (2002) 603-613
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 603-613
    • Chawla-Sarkar, M.1    Leaman, D.W.2    Jacobs, B.S.3    Tuthill, R.J.4    Chatterjee-Kishore, M.5    Stark, G.R.6    Borden, E.C.7
  • 11
    • 7644242953 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells
    • Fribley A., Zeng Q., and Wang C.Y. Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol. Cell. Biol. 24 (2004) 9695-9704
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9695-9704
    • Fribley, A.1    Zeng, Q.2    Wang, C.Y.3
  • 13
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale Jr. M.J., Korth M.J., Tang N.M., Tan S.L., Hopkins D.A., Dever T.E., Polyak S.J., Gretch D.R., and Katze M.G. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230 (1997) 217-227
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale Jr., M.J.1    Korth, M.J.2    Tang, N.M.3    Tan, S.L.4    Hopkins, D.A.5    Dever, T.E.6    Polyak, S.J.7    Gretch, D.R.8    Katze, M.G.9
  • 14
    • 32344442527 scopus 로고    scopus 로고
    • Modulation of PKR activity in cells infected by bovine viral diarrhea virus
    • Gil L.H., van Olphen A.L., Mittal S.K., and Donis R.O. Modulation of PKR activity in cells infected by bovine viral diarrhea virus. Virus Res. 116 (2006) 69-77
    • (2006) Virus Res. , vol.116 , pp. 69-77
    • Gil, L.H.1    van Olphen, A.L.2    Mittal, S.K.3    Donis, R.O.4
  • 15
    • 0035062597 scopus 로고    scopus 로고
    • Noncytolytic control of viral infections by the innate and adaptive immune response
    • Guidotti L.G., and Chisari F.V. Noncytolytic control of viral infections by the innate and adaptive immune response. Annu. Rev. Immunol. 19 (2001) 65-91
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 65-91
    • Guidotti, L.G.1    Chisari, F.V.2
  • 16
    • 33645142635 scopus 로고    scopus 로고
    • Viruses, endoplasmic reticulum stress, and interferon responses
    • He B. Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ. 13 (2006) 393-403
    • (2006) Cell Death Differ. , vol.13 , pp. 393-403
    • He, B.1
  • 17
    • 0028864798 scopus 로고
    • A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons alpha and beta and alters macrophage responses
    • Hwang S.Y., Hertzog P.J., Holland K.A., Sumarsono S.H., Tymms M.J., Hamilton J.A., Whitty G., Bertoncello I., and Kola I. A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons alpha and beta and alters macrophage responses. Proc. Natl. Acad. Sci. USA 92 (1995) 11284-11288
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11284-11288
    • Hwang, S.Y.1    Hertzog, P.J.2    Holland, K.A.3    Sumarsono, S.H.4    Tymms, M.J.5    Hamilton, J.A.6    Whitty, G.7    Bertoncello, I.8    Kola, I.9
  • 18
    • 0025886837 scopus 로고
    • Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons
    • John J., McKendry R., Pellegrini S., Flavell D., Kerr I.M., and Stark G.R. Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons. Mol. Cell. Biol. 11 (1991) 4189-4195
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4189-4195
    • John, J.1    McKendry, R.2    Pellegrini, S.3    Flavell, D.4    Kerr, I.M.5    Stark, G.R.6
  • 19
    • 0034044769 scopus 로고    scopus 로고
    • Interferon beta in multiple sclerosis: is IL-12 suppression the key?
    • Karp C.L., Biron C.A., and Irani D.N. Interferon beta in multiple sclerosis: is IL-12 suppression the key?. Immunol. Today 21 (2000) 24-28
    • (2000) Immunol. Today , vol.21 , pp. 24-28
    • Karp, C.L.1    Biron, C.A.2    Irani, D.N.3
  • 20
    • 0036715591 scopus 로고    scopus 로고
    • Viruses and interferon: a fight for supremacy
    • Katze M.G., He Y., and Gale Jr. M. Viruses and interferon: a fight for supremacy. Nat. Rev. Immunol. 2 (2002) 675-687
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 675-687
    • Katze, M.G.1    He, Y.2    Gale Jr., M.3
  • 21
    • 0036269757 scopus 로고    scopus 로고
    • Cancer immunotherapy: the interferon-alpha experience
    • Kirkwood J. Cancer immunotherapy: the interferon-alpha experience. Semin. Oncol. 29 (2002) 18-26
    • (2002) Semin. Oncol. , vol.29 , pp. 18-26
    • Kirkwood, J.1
  • 22
    • 0142105396 scopus 로고    scopus 로고
    • SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor
    • Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., and Fuchs S.Y. SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor. EMBO J. 22 (2003) 5480-5490
    • (2003) EMBO J. , vol.22 , pp. 5480-5490
    • Kumar, K.G.1    Tang, W.2    Ravindranath, A.K.3    Clark, W.A.4    Croze, E.5    Fuchs, S.Y.6
  • 23
    • 8744247500 scopus 로고    scopus 로고
    • Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor
    • Kumar K.G., Krolewski J.J., and Fuchs S.Y. Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J. Biol. Chem. 279 (2004) 46614-46620
    • (2004) J. Biol. Chem. , vol.279 , pp. 46614-46620
    • Kumar, K.G.1    Krolewski, J.J.2    Fuchs, S.Y.3
  • 25
    • 42549166042 scopus 로고    scopus 로고
    • Raf inhibitor stabilizes receptor for the type I interferon but inhibits its anti-proliferative effects in human malignant melanoma cells
    • Kumar K.G., Liu J., Li Y., Yu D., Thomas-Tikhonenko A., Herlyn M., and Fuchs S.Y. Raf inhibitor stabilizes receptor for the type I interferon but inhibits its anti-proliferative effects in human malignant melanoma cells. Cancer Biol. Ther. 6 (2007) 1437-1441
    • (2007) Cancer Biol. Ther. , vol.6 , pp. 1437-1441
    • Kumar, K.G.1    Liu, J.2    Li, Y.3    Yu, D.4    Thomas-Tikhonenko, A.5    Herlyn, M.6    Fuchs, S.Y.7
  • 26
    • 0036037388 scopus 로고    scopus 로고
    • The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range
    • Langland J.O., and Jacobs B.L. The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range. Virology 299 (2002) 133-141
    • (2002) Virology , vol.299 , pp. 133-141
    • Langland, J.O.1    Jacobs, B.L.2
  • 28
    • 2442765339 scopus 로고
    • Production of an interferon by L cells infected with Western equine encephalomyelitis virus
    • Lockart Jr. R.Z. Production of an interferon by L cells infected with Western equine encephalomyelitis virus. J. Bacteriol. 85 (1963) 556-566
    • (1963) J. Bacteriol. , vol.85 , pp. 556-566
    • Lockart Jr., R.Z.1
  • 29
    • 46549086846 scopus 로고
    • Interaction of an interferon with L cells
    • Lockart Jr. R.Z., and Horn B. Interaction of an interferon with L cells. J. Bacteriol. 85 (1963) 996-1002
    • (1963) J. Bacteriol. , vol.85 , pp. 996-1002
    • Lockart Jr., R.Z.1    Horn, B.2
  • 30
    • 34548648264 scopus 로고    scopus 로고
    • HCV structural proteins interfere with interferon-alpha Jak/STAT signalling pathway
    • Luquin E., Larrea E., Civeira M.P., Prieto J., and Aldabe R. HCV structural proteins interfere with interferon-alpha Jak/STAT signalling pathway. Antiviral Res. 76 (2007) 194-197
    • (2007) Antiviral Res. , vol.76 , pp. 194-197
    • Luquin, E.1    Larrea, E.2    Civeira, M.P.3    Prieto, J.4    Aldabe, R.5
  • 32
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., and Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 18 (2007) 716-731
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 35
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • Nawrocki S.T., Carew J.S., Dunner Jr. K., Boise L.H., Chiao P.J., Huang P., Abbruzzese J.L., and McConkey D.J. Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res. 65 (2005) 11510-11519
    • (2005) Cancer Res. , vol.65 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner Jr., K.3    Boise, L.H.4    Chiao, P.J.5    Huang, P.6    Abbruzzese, J.L.7    McConkey, D.J.8
  • 36
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng E.A., Carlson L.M., Gutman D.M., Harrington Jr. W.J., Lee K.P., and Boise L.H. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107 (2006) 4907-4916
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 37
    • 0034467738 scopus 로고    scopus 로고
    • The human interferon alpha species and receptors
    • Pestka S. The human interferon alpha species and receptors. Biopolymers 55 (2000) 254-287
    • (2000) Biopolymers , vol.55 , pp. 254-287
    • Pestka, S.1
  • 38
    • 0026337403 scopus 로고
    • Transmembrane signalling by interferon-alpha
    • Pfeffer L.M., and Colamonici O.R. Transmembrane signalling by interferon-alpha. Pharmacol. Ther. 52 (1991) 149-157
    • (1991) Pharmacol. Ther. , vol.52 , pp. 149-157
    • Pfeffer, L.M.1    Colamonici, O.R.2
  • 39
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 40
    • 0027214809 scopus 로고
    • The biology and biochemistry of interferon-gamma and its receptor
    • Schreiber R.D., and Farrar M.A. The biology and biochemistry of interferon-gamma and its receptor. Gastroenterol. Jpn. 28 Suppl 4 (1993) 88-94
    • (1993) Gastroenterol. Jpn. , vol.28 , Issue.SUPPL. 4 , pp. 88-94
    • Schreiber, R.D.1    Farrar, M.A.2
  • 41
    • 33646171699 scopus 로고    scopus 로고
    • Divergent roles of IRE1alpha and PERK in the unfolded protein response
    • Schroder M., and Kaufman R.J. Divergent roles of IRE1alpha and PERK in the unfolded protein response. Curr. Mol. Med. 6 (2006) 5-36
    • (2006) Curr. Mol. Med. , vol.6 , pp. 5-36
    • Schroder, M.1    Kaufman, R.J.2
  • 42
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma S., tenOever B.R., Grandvaux N., Zhou G.P., Lin R., and Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science 300 (2003) 1148-1151
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1    tenOever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 44
    • 0034733672 scopus 로고    scopus 로고
    • Cross talk between interferon-gamma and -alpha/beta signaling components in caveolar membrane domains
    • Takaoka A., Mitani Y., Suemori H., Sato M., Yokochi T., Noguchi S., Tanaka N., and Taniguchi T. Cross talk between interferon-gamma and -alpha/beta signaling components in caveolar membrane domains. Science 288 (2000) 2357-2360
    • (2000) Science , vol.288 , pp. 2357-2360
    • Takaoka, A.1    Mitani, Y.2    Suemori, H.3    Sato, M.4    Yokochi, T.5    Noguchi, S.6    Tanaka, N.7    Taniguchi, T.8
  • 45
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • Tardif K.D., Waris G., and Siddiqui A. Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol. 13 (2005) 159-163
    • (2005) Trends Microbiol. , vol.13 , pp. 159-163
    • Tardif, K.D.1    Waris, G.2    Siddiqui, A.3
  • 46
    • 0032818247 scopus 로고    scopus 로고
    • Immunomodulation and therapeutic effects of the oral use of interferon-alpha: mechanism of action
    • Tompkins W.A. Immunomodulation and therapeutic effects of the oral use of interferon-alpha: mechanism of action. J. Interferon Cytokine Res. 19 (1999) 817-828
    • (1999) J. Interferon Cytokine Res. , vol.19 , pp. 817-828
    • Tompkins, W.A.1
  • 47
    • 0026632288 scopus 로고
    • A protein tyrosine kinase in the interferon alpha/beta signaling pathway
    • Velazquez L., Fellous M., Stark G.R., and Pellegrini S. A protein tyrosine kinase in the interferon alpha/beta signaling pathway. Cell 70 (1992) 313-322
    • (1992) Cell , vol.70 , pp. 313-322
    • Velazquez, L.1    Fellous, M.2    Stark, G.R.3    Pellegrini, S.4
  • 48
    • 33747600880 scopus 로고    scopus 로고
    • Causes and consequences of mitochondrial reactive oxygen species generation in hepatitis C
    • Wang T., and Weinman S.A. Causes and consequences of mitochondrial reactive oxygen species generation in hepatitis C. J. Gastroenterol. Hepatol. 21 Suppl 3 (2006) S34-S37
    • (2006) J. Gastroenterol. Hepatol. , vol.21 , Issue.SUPPL. 3
    • Wang, T.1    Weinman, S.A.2
  • 49
    • 0037111954 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3
    • Waris G., Tardif K.D., and Siddiqui A. Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3. Biochem. Pharmacol. 64 (2002) 1425-1430
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1425-1430
    • Waris, G.1    Tardif, K.D.2    Siddiqui, A.3
  • 50
    • 0032780022 scopus 로고    scopus 로고
    • The cellular response to protein misfolding in the endoplasmic reticulum
    • Welihinda A.A., Tirasophon W., and Kaufman R.J. The cellular response to protein misfolding in the endoplasmic reticulum. Gene Expr. 7 (1999) 293-300
    • (1999) Gene Expr. , vol.7 , pp. 293-300
    • Welihinda, A.A.1    Tirasophon, W.2    Kaufman, R.J.3
  • 51
    • 0035005628 scopus 로고    scopus 로고
    • Internally located signal peptides direct hepatitis C virus polyprotein processing in the ER membrane
    • Wu J.Z. Internally located signal peptides direct hepatitis C virus polyprotein processing in the ER membrane. IUBMB Life 51 (2001) 19-23
    • (2001) IUBMB Life , vol.51 , pp. 19-23
    • Wu, J.Z.1
  • 52
    • 47749128073 scopus 로고    scopus 로고
    • ER chaperone regulation, and survival of cells compensating for deficiency in the ER stress response kinase, PERK
    • Yamaguchi Y., Larkin D., Lara-Lemus R., Ramos-Castañeda J., Liu M., and Arvan P. ER chaperone regulation, and survival of cells compensating for deficiency in the ER stress response kinase, PERK. J. Biol. Chem. 283 (2008) 17020-17029
    • (2008) J. Biol. Chem. , vol.283 , pp. 17020-17029
    • Yamaguchi, Y.1    Larkin, D.2    Lara-Lemus, R.3    Ramos-Castañeda, J.4    Liu, M.5    Arvan, P.6
  • 53
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P., McGrath B., Li S., Frank A., Zambito F., Reinert J., Gannon M., Ma K., McNaughton K., and Cavener D.R. The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol. Cell. Biol. 22 (2002) 3864-3874
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 54
    • 30744475504 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response
    • Zheng Y., Gao B., Ye L., Kong L., Jing W., Yang X., and Wu Z. Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response. J. Microbiol. 43 (2005) 529-536
    • (2005) J. Microbiol. , vol.43 , pp. 529-536
    • Zheng, Y.1    Gao, B.2    Ye, L.3    Kong, L.4    Jing, W.5    Yang, X.6    Wu, Z.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.