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Volumn 231, Issue 1, 1997, Pages 81-88

The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of bcl-2, and involves ICE-like proteases

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON; PROTEIN KINASE; PROTEINASE;

EID: 0343812093     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8494     Document Type: Article
Times cited : (117)

References (44)
  • 1
    • 0025815146 scopus 로고
    • Vaccinia virus-encoded eIF-2a homolog abrogates the antiviral effects of interferon
    • Beattie E., Tartaglia J., Paoletti E. Vaccinia virus-encoded eIF-2a homolog abrogates the antiviral effects of interferon. Virology. 183:1991;419-422.
    • (1991) Virology , vol.183 , pp. 419-422
    • Beattie, E.1    Tartaglia, J.2    Paoletti, E.3
  • 2
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M., Grunert S., Murzin A. G., Proctor M., St. Johnston D. NMR solution structure of a dsRNA binding domain from drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14:1995;3563-3571.
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    St. Johnston, D.5
  • 3
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein component of the small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen L. A., Miller D. K., Anhalt G. J., Rosen A. Specific cleavage of the 70-kDa protein component of the small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J. Biol. Chem. 269:1994;30757-30760.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 4
    • 0028881847 scopus 로고
    • DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis
    • Casciola-Rosen L. A., Anhalt G. J., Rosen A. DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J. Exp. Med. 182:1995;1625-1634.
    • (1995) J. Exp. Med. , vol.182 , pp. 1625-1634
    • Casciola-Rosen, L.A.1    Anhalt, G.J.2    Rosen, A.3
  • 5
    • 0029813306 scopus 로고    scopus 로고
    • Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product
    • Dobbelstein M., Shenk T. Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product. J. Virol. 70:1996;6479-6485.
    • (1996) J. Virol. , vol.70 , pp. 6479-6485
    • Dobbelstein, M.1    Shenk, T.2
  • 6
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase
    • Chang H. W., Watson J. C., Jacobs B. L. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 89:1992;4825-4829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4825-4829
    • Chang, H.W.1    Watson, J.C.2    Jacobs, B.L.3
  • 7
    • 0017370502 scopus 로고
    • Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis
    • Farrel P. J., Balkow K., Hunt T., Jackson R. J., Trachsel H. Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis. Cell. 11:1977;187-200.
    • (1977) Cell , vol.11 , pp. 187-200
    • Farrel, P.J.1    Balkow, K.2    Hunt, T.3    Jackson, R.J.4    Trachsel, H.5
  • 8
    • 0026653870 scopus 로고
    • Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase
    • Feng G.-S., Chong K., Kumar A., Williams B. R. G. Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase. Proc. Natl. Acad. Sci. USA. 89:1992;5447-5451.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5447-5451
    • Feng, G.-S.1    Chong, K.2    Kumar, A.3    Williams, B.R.G.4
  • 9
    • 0027105279 scopus 로고
    • Two RNA binding motifs in the double stranded RNA activated protein kinase, DAI
    • Green S. R., Mathews M. B. Two RNA binding motifs in the double stranded RNA activated protein kinase, DAI. Genes Dev. 6:1992;2478-2490.
    • (1992) Genes Dev. , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 10
    • 0028961190 scopus 로고
    • Two functionally distinct RNA binding motifs in the regulatory domain of the protein kinase DAI
    • Green S. R., Manche L., Mathews M. B. Two functionally distinct RNA binding motifs in the regulatory domain of the protein kinase DAI. Mol. Cell Biol. 15:1995;358-364.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 358-364
    • Green, S.R.1    Manche, L.2    Mathews, M.B.3
  • 11
    • 0027421163 scopus 로고
    • Organization of the double-stranded RNA activated protein kinase DAI and virus associated VA RNA1 in adenovirus-2-infected HeLa cells
    • Jimenez-García L. F., Green S. R., Mathews M. B., Spector D. L. Organization of the double-stranded RNA activated protein kinase DAI and virus associated VA RNA1 in adenovirus-2-infected HeLa cells. J. Cell. Sci. 106:1993;11-22.
    • (1993) J. Cell. Sci. , vol.106 , pp. 11-22
    • Jimenez-García, L.F.1    Green, S.R.2    Mathews, M.B.3    Spector, D.L.4
  • 12
    • 0026042013 scopus 로고
    • Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system
    • Katze M. G., Wambach M., Wong M-L., Garfinkel M., Meurs E., Chong K., Williams B. R. G., Hovanessian A. G., Barber G. N. Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system. Mol. Cell. Biol. 11:1991;5497-5505.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5497-5505
    • Katze, M.G.1    Wambach, M.2    Wong, M-L.3    Garfinkel, M.4    Meurs, E.5    Chong, K.6    Williams, B.R.G.7    Hovanessian, A.G.8    Barber, G.N.9
  • 13
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas A. E., Roy S., Barber G. N., Katze M. G., Sonemberg N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science. 257:1992;1685-1689.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonemberg, N.5
  • 14
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-kB by phosphorylating IkB
    • Kumar A. E., Haque J., Lacoste J., Hiscott J., Williams B. R. G. Double-stranded RNA-dependent protein kinase activates transcription factor NF-kB by phosphorylating IkB. Proc. Natl. Acad. Sci. USA. 91:1994;6288-6292.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6288-6292
    • Kumar, A.E.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Williams, B.R.G.5
  • 15
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose)polymerase by a proteinase with properties like ICE
    • Lazebnik Y. A., Kaufman S. H., Desnoyers S., Poirier G. G., Earnshaw W. C. Cleavage of poly(ADP-ribose)polymerase by a proteinase with properties like ICE. Nature. 371:1994;346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufman, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 16
    • 0027157746 scopus 로고
    • The interferon-induced double-stranded RNA-activated human p68 protein kinase inhibits the replication of vaccinia virus
    • Lee S. B., Esteban M. The interferon-induced double-stranded RNA-activated human p68 protein kinase inhibits the replication of vaccinia virus. Virology. 193:1993;1037-1041.
    • (1993) Virology , vol.193 , pp. 1037-1041
    • Lee, S.B.1    Esteban, M.2
  • 17
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee S. B., Esteban M. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology. 199:1994;491-496.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 18
    • 0027943267 scopus 로고
    • Activation of the double-stranded RNA activated human protein kinase in vivo in the absence of its dsRNA binding domain
    • Lee S. B., Green S. R., Mathews M. B., Esteban M. Activation of the double-stranded RNA activated human protein kinase in vivo in the absence of its dsRNA binding domain. Proc. Natl. Acad. Sci. USA. 91:1994;10551-10555.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10551-10555
    • Lee, S.B.1    Green, S.R.2    Mathews, M.B.3    Esteban, M.4
  • 19
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin S. I., Green D. R. Protease activation during apoptosis: Death by a thousand cuts? Cell. 82:1995;349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.I.1    Green, D.R.2
  • 20
    • 0025185463 scopus 로고
    • Induction of apoptosis (programmed cell death) in human leukemia HL-60 cells by inhibition of RNA or protein synthesis
    • Martin S. J., Lennon S. V., Benham A. N., Cotter T. G. Induction of apoptosis (programmed cell death) in human leukemia HL-60 cells by inhibition of RNA or protein synthesis. J. Immunol. 145:1990;1859-1867.
    • (1990) J. Immunol. , vol.145 , pp. 1859-1867
    • Martin, S.J.1    Lennon, S.V.2    Benham, A.N.3    Cotter, T.G.4
  • 21
    • 0001016282 scopus 로고    scopus 로고
    • Interactions between viruses and the cellular machinery for protein synthesis
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press. p. 505-548
    • Mathews M. B. Interactions between viruses and the cellular machinery for protein synthesis. Translational Control. 1996;Cold Spring Harbor Laboratory Press, Cold Spring Harbor. p. 505-548.
    • (1996) Translational Control
    • Mathews, M.B.1
  • 22
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E. F., Chong K., Galabru J., Thomas N. S. B., Kerr I. M., Williams B. R. G., Hovanessian A. G. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell. 62:1990;379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.F.1    Chong, K.2    Galabru, J.3    Thomas, N.S.B.4    Kerr, I.M.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 23
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs E. F, Galabru J., Barber G. N., Katze M. G., Hovanessian A. G. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA. 90:1993;232-236.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 232-236
    • Meurs, E.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 24
    • 0026929934 scopus 로고
    • Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phosphorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth
    • Meurs E. F., Watanabe Y., Kadereit S., Barber G. N., Barber M. G., Chong K., Williams B. R. G., Hovanessian A. G. Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phosphorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth. J. Virol. 66:1992;5805-5814.
    • (1992) J. Virol. , vol.66 , pp. 5805-5814
    • Meurs, E.F.1    Watanabe, Y.2    Kadereit, S.3    Barber, G.N.4    Barber, M.G.5    Chong, K.6    Williams, B.R.G.7    Hovanessian, A.G.8
  • 25
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-B1-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M., Zhu H., Rotello R., Hartwieg E. A., Yuan J-Y. Induction of apoptosis in fibroblasts by IL-B1-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell. 75:1993;653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J-Y.5
  • 27
    • 0030030724 scopus 로고    scopus 로고
    • Mechanism of interferon action: Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells
    • Ortega L. G., McCotter M. D., Henry G. L., McCormack S. J., Thomis D. C., Samuel C. E. Mechanism of interferon action: Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells. Virology. 215:1996;31-39.
    • (1996) Virology , vol.215 , pp. 31-39
    • Ortega, L.G.1    McCotter, M.D.2    Henry, G.L.3    McCormack, S.J.4    Thomis, D.C.5    Samuel, C.E.6
  • 28
    • 0026686791 scopus 로고
    • Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase
    • Patel R. C., Sen G. C. Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase. J. Biol. Chem. 267:1992;7671-7676.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7671-7676
    • Patel, R.C.1    Sen, G.C.2
  • 29
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • Proud C. G. Protein phosphorylation in translational control. Curr. Top. Cell. Regul. 32:1992;243-369.
    • (1992) Curr. Top. Cell. Regul. , vol.32 , pp. 243-369
    • Proud, C.G.1
  • 30
    • 0024316945 scopus 로고
    • Identification of a 90kD polypeptide which associates with adenovirus VA RNA1 and is phosphorylated by the double-stranded RNA dependent protein kinase
    • Rice A. P, Kostura M., Mathews M. B. Identification of a 90kD polypeptide which associates with adenovirus VA RNA1 and is phosphorylated by the double-stranded RNA dependent protein kinase. J. Biol. Chem. 264:1989;20632-20637.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20632-20637
    • Rice, A.P.1    Kostura, M.2    Mathews, M.B.3
  • 31
    • 0025286098 scopus 로고
    • Inducible gene expression from vaccinia virus vectors
    • Rodríguez J. F., Smith G. L. Inducible gene expression from vaccinia virus vectors. Virology. 177:1990;239-250.
    • (1990) Virology , vol.177 , pp. 239-250
    • Rodríguez, J.F.1    Smith, G.L.2
  • 32
    • 0028924758 scopus 로고
    • Structural requirements for dsRNA-binding, dimerization and activation of the human eIF-2a kinase DAI in yeast
    • Romano P. R., Green S. R., Barber G. N., Mathews M. B., Hinnebusch A. G. Structural requirements for dsRNA-binding, dimerization and activation of the human eIF-2a kinase DAI in yeast. Mol. Cell. Biol. 15:1995;365-378.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 365-378
    • Romano, P.R.1    Green, S.R.2    Barber, G.N.3    Mathews, M.B.4    Hinnebusch, A.G.5
  • 33
    • 0040350202 scopus 로고
    • Mechanism of interferon action. Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated protein kinase possessing site-specificity similar to hemin-regulated rabbit reticulocyte kinase
    • Samuel C. E. Mechanism of interferon action. Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated protein kinase possessing site-specificity similar to hemin-regulated rabbit reticulocyte kinase. Proc. Natl. Acad. Sci. USA. 76:1979;600-604.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 600-604
    • Samuel, C.E.1
  • 34
    • 0025739093 scopus 로고
    • Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly antiviral activities
    • Samuel C. E. Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly antiviral activities. Virology. 183:1991;1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 35
    • 0029842883 scopus 로고    scopus 로고
    • Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection
    • Takizawa T., Ohashi K., Nakanishi Y. Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J. Virol. 70:1996;8128-8132.
    • (1996) J. Virol. , vol.70 , pp. 8128-8132
    • Takizawa, T.1    Ohashi, K.2    Nakanishi, Y.3
  • 36
    • 10244257563 scopus 로고    scopus 로고
    • Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR
    • Taylor D. R., Lee S. B., Romano P. R., Marshak D. R., Hinnebusch A. G., Esteban M., Mathews M. B. Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR. Mol. Cell. Biol. 16:1996;6295-6302.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6295-6302
    • Taylor, D.R.1    Lee, S.B.2    Romano, P.R.3    Marshak, D.R.4    Hinnebusch, A.G.5    Esteban, M.6    Mathews, M.B.7
  • 37
    • 0028990125 scopus 로고
    • Yama/CPP32B, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L. T., OŔourke K., Desnoyers S., Zeng Z., Beidler D. R., Poirier G. G., Salvesen G. S., Dixit V. M. Yama/CPP32B, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    Oŕourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 38
    • 0027420488 scopus 로고
    • Mechanism of interferon action: Evidence of intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR
    • Thomis D. C., Samuel C. E. Mechanism of interferon action: Evidence of intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR. J. Virol. 67:1995;7695-7700.
    • (1995) J. Virol. , vol.67 , pp. 7695-7700
    • Thomis, D.C.1    Samuel, C.E.2
  • 39
    • 0027535559 scopus 로고
    • Toward an understanding of the molecular mechanisms of physiological cell death
    • Vaux D. L. Toward an understanding of the molecular mechanisms of physiological cell death. Proc. Natl. Acad. Sci. USA. 90:1993;786-789.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 786-789
    • Vaux, D.L.1
  • 40
    • 0021980039 scopus 로고
    • Double-stranded DNA induces the phosphorylation of several proteins including the 90,000 mol. wt. heat-shock protein in animal cell extracts
    • Walker A. I., Hunt T., Jackson R. J., Anderson C. W. Double-stranded DNA induces the phosphorylation of several proteins including the 90,000 mol. wt. heat-shock protein in animal cell extracts. EMBO J. 4:1985;139-145.
    • (1985) EMBO J. , vol.4 , pp. 139-145
    • Walker, A.I.1    Hunt, T.2    Jackson, R.J.3    Anderson, C.W.4
  • 41
    • 0028168593 scopus 로고
    • Ich-1 and Ice/Ced-3 related genes encode both positive and negative regulators of programmed cell death
    • Wang L., Miura M., Bergenron L., Zhu H., Yuan J. Ich-1 and Ice/Ced-3 related genes encode both positive and negative regulators of programmed cell death. Cell. 78:1994;739-750.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergenron, L.3    Zhu, H.4    Yuan, J.5
  • 42
    • 0025050661 scopus 로고
    • DNA fragmentation induced in macrophages by gliotoxin does not require protein synthesis and is preceded by raised inositol triphosphate levels
    • Waring P. J. DNA fragmentation induced in macrophages by gliotoxin does not require protein synthesis and is preceded by raised inositol triphosphate levels. J. Biol. Chem. 265:1990;14476-14480.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14476-14480
    • Waring, P.J.1
  • 43
    • 0029028320 scopus 로고
    • The last cut is the deepest
    • Whyte M., Evan G. The last cut is the deepest. Nature. 376:1995;17-18.
    • (1995) Nature , vol.376 , pp. 17-18
    • Whyte, M.1    Evan, G.2


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