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Volumn 3, Issue 11, 2011, Pages 2328-2338

Stress granules in the viral replication cycle

Author keywords

eIF2; PKR; Stress; Stress granules

Indexed keywords

INITIATION FACTOR 2; INITIATION FACTOR 2ALPHA; PROTEIN KINASE R; VIRUS PROTEIN;

EID: 82155166803     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v3112328     Document Type: Review
Times cited : (41)

References (49)
  • 1
    • 0030664277 scopus 로고    scopus 로고
    • PKR a protein kinase regulated by double-stranded RNA
    • Clemens, M.J. PKR a protein kinase regulated by double-stranded RNA. Int. J. Biochem. Cell Biol. 1997, 29, 945-949.
    • (1997) Int. J. Biochem. Cell Biol , vol.29 , pp. 945-949
    • Clemens, M.J.1
  • 2
    • 78651488459 scopus 로고    scopus 로고
    • The role of protein kinase R in the interferon response
    • Pindel, A.; Sadler, A. The role of protein kinase R in the interferon response. J. Interferon Cytokine Res. 2011, 31, 59-70.
    • (2011) J. Interferon Cytokine Res , vol.31 , pp. 59-70
    • Pindel, A.1    Sadler, A.2
  • 4
    • 44349125754 scopus 로고    scopus 로고
    • PERK and PKR: Old kinases learn new tricks
    • Raven, J.F.; Koromilas, A.E. PERK and PKR: Old kinases learn new tricks. Cell Cycle 2008, 7, 1146-1150.
    • (2008) Cell Cycle , vol.7 , pp. 1146-1150
    • Raven, J.F.1    Koromilas, A.E.2
  • 5
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor eIF2
    • Kimball, S.R. Eukaryotic initiation factor eIF2. Int. J. Biochem. Cell Biol. 1999, 31, 25-29.
    • (1999) Int. J. Biochem. Cell Biol , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 6
    • 12344305214 scopus 로고    scopus 로고
    • Eif2 and the control of cell physiology
    • Proud, C.G. Eif2 and the control of cell physiology. Semin. Cell Dev. Biol. 2005, 16, 3-12.
    • (2005) Semin. Cell Dev. Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 7
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: EIF2 kinases and translational control
    • Wek, R.C.; Jiang, H.Y.; Anthony, T.G. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 2006, 34, 7-11.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 8
    • 0030267336 scopus 로고    scopus 로고
    • The eIF-2alpha kinases and the control of protein synthesis
    • de Haro, C.; Mendez, R.; Santoyo, J. The eIF-2alpha kinases and the control of protein synthesis. Faseb. J. 1996, 10, 1378-1387.
    • (1996) Faseb. J , vol.10 , pp. 1378-1387
    • de Haro, C.1    Mendez, R.2    Santoyo, J.3
  • 10
    • 0037333760 scopus 로고    scopus 로고
    • Translation initiation and viral tricks
    • Schneider, R.J.; Mohr, I. Translation initiation and viral tricks. Trends. Biochem. Sci. 2003, 28, 130-136.
    • (2003) Trends. Biochem. Sci , vol.28 , pp. 130-136
    • Schneider, R.J.1    Mohr, I.2
  • 11
    • 32644446560 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation events that regulate viral mRNA translation
    • Mohr, I. Phosphorylation and dephosphorylation events that regulate viral mRNA translation. Virus Res. 2006, 119, 89-99.
    • (2006) Virus Res , vol.119 , pp. 89-99
    • Mohr, I.1
  • 12
    • 33646152751 scopus 로고    scopus 로고
    • Antiviral effect of the mammalian translation initiation factor 2alpha kinase GCN2 against RNA viruses
    • Berlanga, J.J.; Ventoso, I.; Harding, H.P.; Deng, J.; Ron, D.; Sonenberg, N.; Carrasco, L.; de Haro, C. Antiviral effect of the mammalian translation initiation factor 2alpha kinase GCN2 against RNA viruses. EMBO J. 2006, 25, 1730-1740.
    • (2006) EMBO J , vol.25 , pp. 1730-1740
    • Berlanga, J.J.1    Ventoso, I.2    Harding, H.P.3    Deng, J.4    Ron, D.5    Sonenberg, N.6    Carrasco, L.7    de Haro, C.8
  • 13
    • 13744253138 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein
    • Cheng, G.; Feng, Z.; He, B. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein. J. Virol. 2005, 79, 1379-1388.
    • (2005) J. Virol , vol.79 , pp. 1379-1388
    • Cheng, G.1    Feng, Z.2    He, B.3
  • 14
    • 0141569267 scopus 로고    scopus 로고
    • Dephosphorylation of eIF-2alpha mediated by the gamma(1)34.5 protein of herpes simplex virus type 1 is required for viral response to interferon but is not sufficient for efficient viral replication
    • Cheng, G.; Yang, K.; He, B. Dephosphorylation of eIF-2alpha mediated by the gamma(1)34.5 protein of herpes simplex virus type 1 is required for viral response to interferon but is not sufficient for efficient viral replication. J. Virol. 2003, 77, 10154-10161.
    • (2003) J. Virol , vol.77 , pp. 10154-10161
    • Cheng, G.1    Yang, K.2    He, B.3
  • 15
    • 29944433224 scopus 로고    scopus 로고
    • Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: A strategy to overcome the antiviral effect of protein kinase PKR
    • Ventoso, I.; Sanz, M.A.; Molina, S.; Berlanga, J.J.; Carrasco, L.; Esteban, M. Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: A strategy to overcome the antiviral effect of protein kinase PKR. Genes Dev. 2006, 20, 87-100.
    • (2006) Genes Dev , vol.20 , pp. 87-100
    • Ventoso, I.1    Sanz, M.A.2    Molina, S.3    Berlanga, J.J.4    Carrasco, L.5    Esteban, M.6
  • 16
    • 0036321944 scopus 로고    scopus 로고
    • Hijacking the translation apparatus by RNA viruses
    • Bushell, M.; Sarnow, P. Hijacking the translation apparatus by RNA viruses. J. Cell Biol. 2002, 158, 395-399.
    • (2002) J. Cell Biol , vol.158 , pp. 395-399
    • Bushell, M.1    Sarnow, P.2
  • 17
    • 0037073485 scopus 로고    scopus 로고
    • Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus
    • Jan, E.; Sarnow, P. Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus. J. Mol. Biol. 2002, 324, 889-902.
    • (2002) J. Mol. Biol , vol.324 , pp. 889-902
    • Jan, E.1    Sarnow, P.2
  • 18
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase
    • Srivastava, S.P.; Kumar, K.U.; Kaufman, R.J. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 1998, 273, 2416-2423.
    • (1998) J. Biol. Chem , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 20
    • 41849103099 scopus 로고    scopus 로고
    • P bodies, stress granules, and viral life cycles
    • Beckham, C.J.; Parker, R. P bodies, stress granules, and viral life cycles. Cell Host Microbe 2008, 3, 206-212.
    • (2008) Cell Host Microbe , vol.3 , pp. 206-212
    • Beckham, C.J.1    Parker, R.2
  • 21
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha, N.; Anderson, P. Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 2002, 30, 963-969.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 23
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto, K.; Fukuda, H.; Imajoh-Ohmi, S.; Saito, H.; Takekawa, M. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat. Cell Biol. 2008, 10, 1324-1332.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 24
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha, N.L.; Gupta, M.; Li, W.; Miller, I.; Anderson, P. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 1999, 147, 1431-1442.
    • (1999) J. Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 25
    • 33749493493 scopus 로고    scopus 로고
    • Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation
    • Mazroui, R.; Sukarieh, R.; Bordeleau, M.E.; Kaufman, R.J.; Northcote, P.; Tanaka, J.; Gallouzi, I.; Pelletier, J. Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation. Mol. Biol. Cell 2006, 17, 4212-4219.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4212-4219
    • Mazroui, R.1    Sukarieh, R.2    Bordeleau, M.E.3    Kaufman, R.J.4    Northcote, P.5    Tanaka, J.6    Gallouzi, I.7    Pelletier, J.8
  • 26
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn, T.; Kedersha, N.; Hickman, T.; Tisdale, S.; Anderson, P. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat. Cell Biol. 2008, 10, 1224-1231.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 28
    • 33845950751 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A
    • Dang, Y.; Kedersha, N.; Low, W.K.; Romo, D.; Gorospe, M.; Kaufman, R.; Anderson, P.; Liu, J.O. Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A. J. Biol. Chem. 2006, 281, 32870-32878.
    • (2006) J. Biol. Chem , vol.281 , pp. 32870-32878
    • Dang, Y.1    Kedersha, N.2    Low, W.K.3    Romo, D.4    Gorospe, M.5    Kaufman, R.6    Anderson, P.7    Liu, J.O.8
  • 29
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha, N.; Chen, S.; Gilks, N.; Li, W.; Miller, I.J.; Stahl, J.; Anderson, P. Evidence that ternary complex (eIF2-GTP-tRNA(i)(met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol. Biol. Cell 2002, 13, 195-210.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Anderson, P.7
  • 30
    • 33947210861 scopus 로고    scopus 로고
    • Distinct structural features of caprin-1 mediate its interaction with G3BP-1 and its induction of phosphorylation of eukaryotic translation initiation factor 2alpha, entry to cytoplasmic stress granules, and selective interaction with a subset of mRNAs
    • Solomon, S.; Xu, Y.; Wang, B.; David, M.D.; Schubert, P.; Kennedy, D.; Schrader, J.W. Distinct structural features of caprin-1 mediate its interaction with G3BP-1 and its induction of phosphorylation of eukaryotic translation initiation factor 2alpha, entry to cytoplasmic stress granules, and selective interaction with a subset of mRNAs. Mol. Cell. Biol. 2007, 27, 2324-2342.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2324-2342
    • Solomon, S.1    Xu, Y.2    Wang, B.3    David, M.D.4    Schubert, P.5    Kennedy, D.6    Schrader, J.W.7
  • 31
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs
    • Nover, L.; Scharf, K.D.; Neumann, D. Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs. Mol. Cell. Biol. 1989, 9, 1298-1308.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 1298-1308
    • Nover, L.1    Scharf, K.D.2    Neumann, D.3
  • 32
    • 0023941655 scopus 로고
    • Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts
    • Collier, N.C.; Heuser, J.; Levy, M.A.; Schlesinger, M.J. Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts. J. Cell Biol. 1988, 106, 1131-1139.
    • (1988) J. Cell Biol , vol.106 , pp. 1131-1139
    • Collier, N.C.1    Heuser, J.2    Levy, M.A.3    Schlesinger, M.J.4
  • 33
    • 77956621599 scopus 로고    scopus 로고
    • Mrna escape from stress granule sequestration is dictated by localization to the endoplasmic reticulum
    • Unsworth, H.; Raguz, S.; Edwards, H.J.; Higgins, C.F.; Yague, E. mRNA escape from stress granule sequestration is dictated by localization to the endoplasmic reticulum. FASEB J. 2010, 24, 3370-3380.
    • (2010) FASEB J , vol.24 , pp. 3370-3380
    • Unsworth, H.1    Raguz, S.2    Edwards, H.J.3    Higgins, C.F.4    Yague, E.5
  • 34
  • 35
  • 37
    • 0032530480 scopus 로고    scopus 로고
    • Proteolysis of human eukaryotic translation initiation factor eIF4GII, but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection
    • Gradi, A.; Svitkin, Y.V.; Imataka, H.; Sonenberg, N. Proteolysis of human eukaryotic translation initiation factor eIF4GII, but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 11089-11094.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 11089-11094
    • Gradi, A.1    Svitkin, Y.V.2    Imataka, H.3    Sonenberg, N.4
  • 38
    • 0842347402 scopus 로고    scopus 로고
    • Cleavage of poly(a)-binding protein by poliovirus 3C protease inhibits host cell translation: A novel mechanism for host translation shutoff
    • Kuyumcu-Martinez, N.M.; Van Eden, M.E.; Younan, P.; Lloyd, R.E. Cleavage of poly(a)-binding protein by poliovirus 3C protease inhibits host cell translation: A novel mechanism for host translation shutoff. Mol. Cell Biol. 2004, 24, 1779-1790.
    • (2004) Mol. Cell Biol , vol.24 , pp. 1779-1790
    • Kuyumcu-Martinez, N.M.1    van Eden, M.E.2    Younan, P.3    Lloyd, R.E.4
  • 39
    • 77949389673 scopus 로고    scopus 로고
    • Stable formation of compositionally unique stress granules in virus-infected cells
    • Piotrowska, J.; Hansen, S.J.; Park, N.; Jamka, K.; Sarnow, P.; Gustin, K.E. Stable formation of compositionally unique stress granules in virus-infected cells. J. Virol. 2010, 84, 3654-3665.
    • (2010) J. Virol , vol.84 , pp. 3654-3665
    • Piotrowska, J.1    Hansen, S.J.2    Park, N.3    Jamka, K.4    Sarnow, P.5    Gustin, K.E.6
  • 40
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White, J.P.; Cardenas, A.M.; Marissen, W.E.; Lloyd, R.E. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2007, 2, 295-305.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 41
    • 70350678748 scopus 로고    scopus 로고
    • Mammalian orthoreovirus particles induce and are recruited into stress granules at early times postinfection
    • Qin, Q.; Hastings, C.; Miller, C.L. Mammalian orthoreovirus particles induce and are recruited into stress granules at early times postinfection. J. Virol. 2009, 83, 11090-11101.
    • (2009) J. Virol , vol.83 , pp. 11090-11101
    • Qin, Q.1    Hastings, C.2    Miller, C.L.3
  • 42
    • 34547883878 scopus 로고    scopus 로고
    • Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies
    • Raaben, M.; Groot Koerkamp, M.J.; Rottier, P.J.; de Haan, C.A. Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies. Cell. Microbiol. 2007, 9, 2218-2229.
    • (2007) Cell. Microbiol , vol.9 , pp. 2218-2229
    • Raaben, M.1    Groot, K.M.J.2    Rottier, P.J.3    de Haan, C.A.4
  • 43
    • 79953107370 scopus 로고    scopus 로고
    • Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication
    • Lindquist, M.E.; Mainou, B.A.; Dermody, T.S.; Crowe, J.E., Jr. Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication. Virology 2011, 413, 103-110.
    • (2011) Virology , vol.413 , pp. 103-110
    • Lindquist, M.E.1    Mainou, B.A.2    Dermody, T.S.3    Crowe Jr., J.E.4
  • 44
    • 78049506923 scopus 로고    scopus 로고
    • Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication
    • Lindquist, M.E.; Lifland, A.W.; Utley, T.J.; Santangelo, P.J.; Crowe, J.E., Jr. Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication. J. Virol. 2010, 84, 12274-12284.
    • (2010) J. Virol , vol.84 , pp. 12274-12284
    • Lindquist, M.E.1    Lifland, A.W.2    Utley, T.J.3    Santangelo, P.J.4    Crowe Jr., J.E.5
  • 45
    • 80052963807 scopus 로고    scopus 로고
    • The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6
    • Legros, S.; Boxus, M.; Gatot, J.S.; Van Lint, C.; Kruys, V.; Kettmann, R.; Twizere, J.C.; Dequiedt, F. The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6. Oncogene 2011, 30, 4050-4062.
    • (2011) Oncogene , vol.30 , pp. 4050-4062
    • Legros, S.1    Boxus, M.2    Gatot, J.S.3    van Lint, C.4    Kruys, V.5    Kettmann, R.6    Twizere, J.C.7    Dequiedt, F.8
  • 46
    • 34547456097 scopus 로고    scopus 로고
    • Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
    • Emara, M.M.; Brinton, M.A. Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 9041-9046.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 9041-9046
    • Emara, M.M.1    Brinton, M.A.2
  • 47
    • 0036888883 scopus 로고    scopus 로고
    • Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication
    • Li, W.; Li, Y.; Kedersha, N.; Anderson, P.; Emara, M.; Swiderek, K.M.; Moreno, G.T.; Brinton, M.A. Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J. Virol. 2002, 76, 11989-12000.
    • (2002) J. Virol , vol.76 , pp. 11989-12000
    • Li, W.1    Li, Y.2    Kedersha, N.3    Anderson, P.4    Emara, M.5    Swiderek, K.M.6    Moreno, G.T.7    Brinton, M.A.8
  • 48
    • 77957200555 scopus 로고    scopus 로고
    • Is responsible for the phosphorylation of eIF2alpha in rotavirus infection
    • Rojas, M.; Arias, C.F.; Lopez, S. Protein kinase R is responsible for the phosphorylation of eIF2alpha in rotavirus infection. J. Virol. 2010, 84, 10457-10466.
    • (2010) J. Virol , vol.84 , pp. 10457-10466
    • Rojas, M.1    Arias, C.F.2    Lopez, S.3    Protein, K.R.4
  • 49
    • 38349138566 scopus 로고    scopus 로고
    • Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules
    • Montero, H.; Rojas, M.; Arias, C.F.; Lopez, S. Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules. J. Virol. 2008, 82, 1496-1504.
    • (2008) J. Virol , vol.82 , pp. 1496-1504
    • Montero, H.1    Rojas, M.2    Arias, C.F.3    Lopez, S.4


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