Inhibition of Double-Stranded RNA- and Tumor Necrosis Factor Alpha-Mediated Apoptosis by Tetratricopeptide Repeat Protein and Cochaperone P58^IPK

REFERENCES

• Abraham, N., D. F. Stojdl, P. I. Duncan, N. Méthot, T. Ishii, M. Dubé, B. C. Vanderhyden, H. L. Atkins, D. A. Gray, M. W. McBurney, A. E. Koromilas, E. G. Brown, N. Sonenberg, and J. Bell 1999. Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR. J. Biol. Chem. 274:5953–5962.
   PubMedGoogle Scholar
• Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, K. Struhl 1988. Current protocols in molecular biology. John Wiley & Sons, Inc., New York, N.Y.
   Google Scholar
• Balachandran, S., C. N. Kim, W.-C. Yeh, T. W. Mak, and J. Barber 1998. Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling. EMBO J. 17:6888–6902.
   PubMed Web of Science ®Google Scholar
• Barber, G. N., R. Jagus, E. F. Meurs, A. G. Hovanessian, and J. Katze 1995. Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase. J. Biol. Chem. 270:17423–17428.
   PubMedGoogle Scholar
• Barber, G. N., S. Thompson, T. G. Lee, T. Strom, R. Jagus, A. Darveau, and J. Katze 1994. The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties. Proc. Natl. Acad. Sci. USA 91:4278–4282.
   PubMedGoogle Scholar
• Barber, G. N., M. Wambach, S. Thompson, R. Jagus, and J. Katze 1995. Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation. Mol. Cell. Biol. 15:3138–3146.
   PubMedGoogle Scholar
• Bertin, J., R. C. Armstrong, S. Ottilie, D. A. Martin, Y. Wang, S. Banks, G.-H. Wang, T. G. Senkevich, E. S. Alnemri, B. Moss, M. J. Lenardo, K. J. Tomaselli, and J. Cohen 1997. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. Proc. Natl. Acad. Sci. USA 94:1172–1176.
   PubMed Web of Science ®Google Scholar
• Cheetham, M. E., and J. Caplan 1998. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3:28–36.
   PubMed Web of Science ®Google Scholar
• Cheng, E. H. Y., J. Nicholas, D. S. Bellows, G. S. Hayward, H. G. Guo, M. S. Reitz, and J. Hardwick 1997. A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. Proc. Natl. Acad. Sci. USA 94:690–694.
   PubMed Web of Science ®Google Scholar
• Chou, J., and J. Roizman 1992. The γ134.5 gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programmed cell death in neuronal cells. Proc. Natl. Acad. Sci. USA 89:3266–3270.
   PubMed Web of Science ®Google Scholar
• Cohen, G. M. 1997. Caspases: the executioners of apoptosis. Biochem. J. 326:1–16.
   PubMed Web of Science ®Google Scholar
• Der, S. D., Y.-L. Yang, C. Weissman, and J. Williams 1997. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 94:3279–3283.
   PubMed Web of Science ®Google Scholar
• Donzé, O., R. Jagus, A. E. Koromilas, J. W. B. Hershey, and J. Sonenberg 1995. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J. 14:3828–3834.
   PubMed Web of Science ®Google Scholar
• Finco, T. S., A. S. Baldwin Jr.. 1993. κB site-dependent induction of gene expression by diverse inducers of nuclear factor κB requires Raf-1. J. Biol. Chem. 268:17676–17679.
   PubMed Web of Science ®Google Scholar
• Galang, C. K., J. J. García-Ramírez, P. A. Solski, J. K. Westwick, C. J. Der, N. N. Neznanov, and J. Oshima 1996. Oncogenic Neu/Erb-2 increases Ets, AP-1, and NF-κB-dependent gene expression, and inhibiting Ets activation blocks Neu-mediated cellular transformation. J. Biol. Chem. 271:7992–7998.
   PubMed Web of Science ®Google Scholar
• Galang, C. K., C. J. Der, and J. Hauser 1994. Oncogenic Ras can induce transcriptional activation through a variety of promoter elements, including tandem c-Ets-2 binding sites. Oncogene 9:2913–2921.
   PubMed Web of Science ®Google Scholar
• Gale, M. Jr., C. M. Blakely, D. A. Hopkins, M. W. Melville, M. Wambach, P. R. Romano, and J. Katze 1998. Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK. Mol. Cell. Biol. 18:859–871.
   PubMedGoogle Scholar
• Gale, M. Jr., S.-L. Tan, M. Wambach, and J. Katze 1996. Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation. Mol. Cell. Biol. 16:4172–4181.
   PubMedGoogle Scholar
• Haque, S. J., and J. Williams 1994. Identification and characterization of an interferon (IFN)-stimulated response element-IFN-stimulated gene factor 3-independent signaling pathway for IFN-α. J. Biol. Chem. 269:19523–19529.
   PubMedGoogle Scholar
• Hardwick, J. M. 1997. Virus-induced apoptosis. Adv. Pharmacol. 41:295–336.
   PubMedGoogle Scholar
• He, B., M. Gross, and J. Roizman 1997. The γ34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α 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. USA 94:843–848.
   PubMed Web of Science ®Google Scholar
• Hinshaw, V. S., C. W. Olsen, N. Dybdahl-Sissoko, and J. Evans 1994. Apoptosis: a mechanism of cell killing by influenza A and B viruses. J. Virol. 68:3667–3673.
   PubMed Web of Science ®Google Scholar
• Höhfeld, J. 1998. Regulation of the heat shock cognate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol. Chem. 379:269–274.
   PubMed Web of Science ®Google Scholar
• Höhfeld, J., and J. Jentsch 1997. GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16:6209–6216.
   PubMed Web of Science ®Google Scholar
• Huang, D. C. S., S. Cory, and J. Strasser 1997. Bcl-1, Bcl-x(1) and adenovirus EIB19k are functionally equivalent in their ability to inhibit cell death. Oncogene 14:405–414.
   PubMed Web of Science ®Google Scholar
• Kibler, K. V., T. Shors, K. B. Perkins, C. C. Zeman, M. P. Banaszak, J. Biesterfeldt, J. O. Langland, and J. Jacobs 1997. Double-stranded RNA is a trigger for apoptosis in vaccinia virus-infected cells. J. Virol. 71:1992–2003.
   PubMed Web of Science ®Google Scholar
• Koromilas, A. E., S. Roy, G. N. Barber, M. G. Katze, and J. Sonenberg 1992. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257:1685–1689.
   PubMed Web of Science ®Google Scholar
• Kumar, A., Y.-L. Yang, V. Flati, S. Der, S. Kadereit, A. Deb, J. Haque, L. Reis, C. Weissmann, and J. Williams 1997. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-κB. EMBO J. 16:406–416.
   PubMed Web of Science ®Google Scholar
• Lee, S. B., and J. Esteban 1994. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology 199:491–496.
   PubMed Web of Science ®Google Scholar
• Lee, S. B., D. Rodríguez, J. R. Rodríguez, and J. Esteban 1997. 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. Virology 231:81–88.
   PubMed Web of Science ®Google Scholar
• Lee, T. G., N. Tang, S. Thompson, J. Miller, and J. Katze 1994. The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol. Cell. Biol. 14:2331–2342.
   PubMedGoogle Scholar
• Lee, T. G., J. Tomita, A. G. Hovanessian, and J. Katze 1990. Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells. Proc. Natl. Acad. Sci. USA 87:6208–6212.
   PubMed Web of Science ®Google Scholar
• Lee, T. G., J. Tomita, A. G. Hovanessian, and J. Katze 1992. Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase. J. Biol. Chem. 267:14238–14243.
   PubMed Web of Science ®Google Scholar
• Maran, A., R. K. Maitra, A. Kumar, B. Dong, W. Xiao, G. Li, B. R. G. Williams, P. F. Torrence, and J. Silverman 1994. Blockage of NF-κB signaling by selective ablation of an mRNA target by 2-5A antisense chimeras. Science 265:789–792.
   PubMed Web of Science ®Google Scholar
• Melville, M. W., W. J. Hansen, B. C. Freeman, W. J. Welch, and J. Katze 1997. The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR. Proc. Natl. Acad. Sci. USA 94:97–102.
   PubMedGoogle Scholar
• Melville, M. W., S.-L. Tan, M. Wambach, J. Song, R. I. Morimoto, and J. Katze 1999. The cellular inhibitor of the PKR protein kinase, P58IPK, is an influenza virus-activated co-chaperone that modulates heat shock protein to activity. J. Biol. Chem. 274:3797–3803.
   PubMedGoogle Scholar
• Meurs, E. F., J. Galabru, G. N. Barber, M. G. Katze, and J. Hovanessian 1993. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 90:232–236.
   PubMed Web of Science ®Google Scholar
• O’Brien, V. 1998. Viruses and apoptosis. J. Gen. Virol. 79:1833–1845.
   PubMed Web of Science ®Google Scholar
• Pratt, W. B. 1998. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med. 217:420–434.
   PubMed Web of Science ®Google Scholar
• Savinova, O., and J. Jagus 1997. Use of vertical slab isoelectric focusing and immunoblotting to evaluate steady-state phosphorylation of eIF-2α in cultured cells. Methods: Companion Methods Enzymol. 11:419–425.
   Google Scholar
• Scheffner, M., B. A. Werness, J. M. Huibregstse, A. J. Levine, and J. Howley 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63:1129–1136.
   PubMed Web of Science ®Google Scholar
• Smith, D. F. 1998. Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes. Biol. Chem. 379:283–288.
   PubMedGoogle Scholar
• Srinivasula, S. M., M. Ahmad, T. Fernandes-Alnemri, G. Litwack, and J. Alnemri 1996. Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci. USA 93:14486–14491.
   PubMed Web of Science ®Google Scholar
• Srivastava, S. P., K. U. Kumar, and J. Kaufman 1998. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 273:2416–2423.
   PubMed Web of Science ®Google Scholar
• Takayama, S., D. N. Bimston, S. Matsuzawa, B. C. Freeman, C. Aime-Sempe, Z. Xie, R. I. Morimoto, and J. Reed 1997. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. EMBO J. 16:4887–4896.
   PubMed Web of Science ®Google Scholar
• Takizawa, T., S. Matsukawa, Y. Higuchi, S. Nakamura, Y. Nakanishi, and J. Fukuda 1993. Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells. J. Gen. Virol. 74:2347–2355.
   PubMed Web of Science ®Google Scholar
• Takizawa, T., K. Ohashi, and J. Nakanishi 1996. Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J. Virol. 70:8128–8132.
   PubMed Web of Science ®Google Scholar
• Tan, S.-L., M. J. Gale Jr., and J. Katze 1998. Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor. Mol. Cell. Biol. 18:2431–2443.
   PubMedGoogle Scholar
• Tan, S.-L., and M. G. Katze. The emerging role of the interferon-induced PKR protein kinase as an apoptotic effector: a new face of death? J. Interferon Cytokine Res., in press.
   Google Scholar
• Tang, N. M., C. Y. Ho, and J. Katze 1996. The 58-kDa cellular inhibitor of the double stranded RNA-dependent protein kinase requires the tetratricopeptide repeat 6 and DnaJ motifs to stimulate protein synthesis in vivo. J. Biol. Chem. 271:28660–28666.
   PubMedGoogle Scholar
• Teodoro, J. G., and J. Branton 1997. Regulation of apoptosis by viral gene products. J. Virol. 71:1739–1746.
   PubMed Web of Science ®Google Scholar
• Tewari, M., W. G. Telford, R. A. Miller, and J. Dixit 1995. CrmA, a poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis. J. Biol. Chem. 270:22705–22708.
   PubMedGoogle Scholar
• Thome, M., P. Schneider, K. Hofmann, H. Fickenscher, E. Meinl, F. Neipel, C. Mattmann, K. Burns, J.-L. Bodmer, M. Schroter, C. Scaffidi, P. H. Krammer, and J. Peter 1997. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386:517–521.
   PubMed Web of Science ®Google Scholar
• Towbin, H., T. Staehlin, and J. Gordon 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and applications. Proc. Natl. Acad. Sci. USA 76:4350–4354.
   PubMed Web of Science ®Google Scholar
• Yang, Y.-L., L. F. L. Reis, J. Pavlovic, A. Aguzzi, R. Schäfer, A. Kumar, B. R. G. Williams, M. Aguet, and J. Weissmann 1995. Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase. EMBO J. 14:6095–6106.
   PubMed Web of Science ®Google Scholar
• Yeung, M. C., and J. Lau 1998. Tumor suppressor p53 as a component of the tumor necrosis factor-induced, protein kinase PKR-mediated apoptotic pathway in human promonocytic U937 cells. J. Biol. Chem. 273:25198–25202.
   PubMed Web of Science ®Google Scholar
• Yeung, M. C., J. Liu, and J. Lau 1996. An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells. Proc. Natl. Acad. Sci. USA 93:12451–12455.
   PubMed Web of Science ®Google Scholar