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Volumn 2, Issue 9, 2011, Pages

Cell death regulation during influenza A virus infection by matrix (M1) protein: A model of viral control over the cellular survival pathway

Author keywords

Apaf 1; Apoptosis; Caspase 9; Hsp70; Influenza A virus; Matrix 1 protein

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; DEOXYADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 70; MATRIX PROTEIN; PROCASPASE 9; PROTEIN MATRIX 1; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 80053400600     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2011.75     Document Type: Article
Times cited : (42)

References (40)
  • 1
    • 0035094982 scopus 로고    scopus 로고
    • Host defense, viruses and apoptosis
    • DOI 10.1038/sj.cdd.4400823
    • Barber GN. Host defense, viruses and apoptosis. Cell Death Differ 2001; 8: 113-126. (Pubitemid 32201359)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.2 , pp. 113-126
    • Barber, G.N.1
  • 2
    • 0035090326 scopus 로고    scopus 로고
    • Apoptosis in viral pathogenesis
    • DOI 10.1038/sj.cdd.4400820
    • Hardwick JM. Apoptosis in viral pathogenesis. Cell Death Differ 2001; 8: 109-110. (Pubitemid 32201358)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.2 , pp. 109-110
    • Hardwick, J.M.1
  • 3
    • 77958184901 scopus 로고    scopus 로고
    • Manipulation of host cell death pathways during microbial infections
    • Lamkanfi M, Dixit VM. Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 2010; 8: 44-54.
    • (2010) Cell Host Microbe , vol.8 , pp. 44-54
    • Lamkanfi, M.1    Dixit, V.M.2
  • 4
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: Viral evasion of apoptosis
    • DOI 10.1038/ni1102-1013
    • Benedict CA, Norris PS, Ware CF. To kill or be killed: viral evasion of apoptosis. Nat Immunol 2002; 3: 1013-1018. (Pubitemid 35363651)
    • (2002) Nature Immunology , vol.3 , Issue.11 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 5
    • 77953306075 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein 1 suppresses virus-induced cellular apoptosis to facilitate viral growth by activating the cell survival pathways during early stages of infection
    • Bagchi P, Dutta D, Chattopadhyay S, Mukherjee A, Halder UC, Sarkar S et al. Rotavirus nonstructural protein 1 suppresses virus-induced cellular apoptosis to facilitate viral growth by activating the cell survival pathways during early stages of infection. J Virol 2010; 84: 6834-6845.
    • (2010) J Virol , vol.84 , pp. 6834-6845
    • Bagchi, P.1    Dutta, D.2    Chattopadhyay, S.3    Mukherjee, A.4    Halder, U.C.5    Sarkar, S.6
  • 6
    • 65549130101 scopus 로고    scopus 로고
    • A new player in a deadly game: Influenza viruses and the PI3K/Akt signalling pathway
    • Ehrhardt C, Ludwig S. A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway. Cell Microbiol 2009; 11: 863-871.
    • (2009) Cell Microbiol , vol.11 , pp. 863-871
    • Ehrhardt, C.1    Ludwig, S.2
  • 7
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 2009; 16: 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 8
    • 68749118090 scopus 로고    scopus 로고
    • The molecular chaperone heat shock protein-90 positively regulates rotavirus infection
    • Dutta D, Bagchi P, Chatterjee A, Nayak MK, Mukherjee A, Chattopadhyay S et al. The molecular chaperone heat shock protein-90 positively regulates rotavirus infection. Virology 2009; 391: 325-333.
    • (2009) Virology , vol.391 , pp. 325-333
    • Dutta, D.1    Bagchi, P.2    Chatterjee, A.3    Nayak, M.K.4    Mukherjee, A.5    Chattopadhyay, S.6
  • 9
    • 0034648790 scopus 로고    scopus 로고
    • Activation of heat-shock response by an adenovirus is essential for virus replication
    • Glotzer JB, Saltik M, Chiocca S, Michou AI, Moseley P, Cotton M. Activation of heat-shock response by an adenovirus is essential for virus replication. Nature 2000; 407: 207-211.
    • (2000) Nature , vol.407 , pp. 207-211
    • Glotzer, J.B.1    Saltik, M.2    Chiocca, S.3    Michou, A.I.4    Moseley, P.5    Cotton, M.6
  • 10
    • 0036723643 scopus 로고    scopus 로고
    • Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein
    • Lin BY, Makhov AM, Griffith JD, Broker TR, Chow LT. Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein. Mol Cell Biol 2002; 22: 6592-6604.
    • (2002) Mol Cell Biol , vol.22 , pp. 6592-6604
    • Lin, B.Y.1    Makhov, A.M.2    Griffith, J.D.3    Broker, T.R.4    Chow, L.T.5
  • 12
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
    • DOI 10.1074/jbc.M405627200
    • Ben-Zvi A, De Los Rios P, Dietler G, Goloubinoff P. Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J Biol Chem 2004; 279: 37298-37303. (Pubitemid 39195436)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 13
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, Mosser DD, Mahboubi A, Kuwana T et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000; 2: 469-475.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3    Mosser, D.D.4    Mahboubi, A.5    Kuwana, T.6
  • 14
    • 43049147998 scopus 로고    scopus 로고
    • PHAPI, CAS, and Hsp70 Promote Apoptosome Formation by Preventing Apaf-1 Aggregation and Enhancing Nucleotide Exchange on Apaf-1
    • DOI 10.1016/j.molcel.2008.03.014, PII S1097276508002384
    • Kim HE, Jiang X, Du F, Wang X. PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1. Mol Cell 2008; 30: 239-247. (Pubitemid 351626690)
    • (2008) Molecular Cell , vol.30 , Issue.2 , pp. 239-247
    • Kim, H.-E.1    Jiang, X.2    Du, F.3    Wang, X.4
  • 16
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • DOI 10.1128/JVI.01917-06
    • Naito T, Momose F, Kawaguchi A, Nagata K. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J Virol 2007; 81: 1339-1349. (Pubitemid 46167855)
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 17
    • 0347003598 scopus 로고    scopus 로고
    • Heat Shock Protein 70 Is Related to Thermal Inhibition of Nuclear Export of the Influenza Virus Ribonucleoprotein Complex
    • DOI 10.1128/JVI.78.3.1263-1270.2004
    • Hirayama E, Atagi H, Hiraki A, Kim J. Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex. J Virol 2004; 78: 1263-1270. (Pubitemid 38095836)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1263-1270
    • Hirayama, E.1    Atagi, H.2    Hiraki, A.3    Kim, J.4
  • 18
    • 0033557045 scopus 로고    scopus 로고
    • Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site
    • DOI 10.1006/viro.1998.9555
    • Shimizu K, Iguchi A, Gomyou R, Ono Y. Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site. Virology 1999; 254: 213-219. (Pubitemid 29393319)
    • (1999) Virology , vol.254 , Issue.2 , pp. 213-219
    • Shimizu, K.1    Iguchi, A.2    Gomyou, R.3    Yasushi, O.4
  • 21
    • 33846160497 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K
    • DOI 10.1099/vir.0.82419-0
    • Shin YK, Liu Q, Tikoo SK, Babiuk LA, Zhou Y. Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. J Gen Virol 2007; 88: 13-18. (Pubitemid 46085109)
    • (2007) Journal of General Virology , vol.88 , Issue.1 , pp. 13-18
    • Shin, Y.-K.1    Liu, Q.2    Tikoo, S.K.3    Babiuk, L.A.4    Zhou, Y.5
  • 23
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin D, Garc?́a-Sastre A, Xiao X, Wang R, Palese P. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog 2005; 1: e4.
    • (2005) PLoS Pathog , vol.1
    • Zamarin, D.1    Garća-Sastre, A.2    Xiao, X.3    Wang, R.4    Palese, P.5
  • 25
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein: Interfaces can rotate in the oligomeric structures of M1
    • DOI 10.1006/viro.2001.1119
    • Harris A, Forouhar F, Qiu S, Sha B, Luo M. The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 2001; 289: 34-44. (Pubitemid 33016235)
    • (2001) Virology , vol.289 , Issue.1 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 26
    • 33749338927 scopus 로고    scopus 로고
    • Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle
    • DOI 10.1016/j.febslet.2006.09.040, PII S0014579306011501
    • Watanabe K, Fuse T, Asano I, Tsukahara F, Maru Y, Nagata K. Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle. FEBS Lett 2006; 580: 5785-5790. (Pubitemid 44498679)
    • (2006) FEBS Letters , vol.580 , Issue.24 , pp. 5785-5790
    • Watanabe, K.1    Fuse, T.2    Asano, I.3    Tsukahara, F.4    Maru, Y.5    Nagata, K.6    Kitazato, K.7    Kobayashi, N.8
  • 28
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005; 62: 670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 29
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-489. (Pubitemid 27508237)
    • (1997) Cell , vol.91 , Issue.4 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 30
    • 0021381689 scopus 로고
    • Herpes simplex virus infection causes the accumulation of a heat-shock protein
    • LaThangue NB, Shriver K, Dawson C, Chan WL. Herpes simplex virus infection causes the accumulation of a heat-shock protein. EMBO J 1984; 3: 267-277.
    • (1984) EMBO J , vol.3 , pp. 267-277
    • Lathangue, N.B.1    Shriver, K.2    Dawson, C.3    Chan, W.L.4
  • 31
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman BC, Myers MP, Schumacher R, Morimoto RI. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 1995; 14: 2281-2292.
    • (1995) EMBO J , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 32
    • 0024535928 scopus 로고
    • Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells
    • Hatada E, Hasegawa M, Mukaigawa J, Shimizu K, Fukuda R. Control of influenza virus gene expression: quantitative analysis of each viral RNA species in infected cells. J Biochem (Tokyo) 1989; 105: 537-546. (Pubitemid 19106773)
    • (1989) Journal of Biochemistry , vol.105 , Issue.4 , pp. 537-546
    • Hatada, E.1    Hasegawa, M.2    Mukaigawa, J.3    Shimizu, K.4    Fukuda, R.5
  • 33
    • 16444378781 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: A crucial part of viral survival strategies
    • DOI 10.1007/s10254-004-0025-5
    • Mayer MP. Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev Physiol Biochem Pharmacol 2005; 153: 1-46. (Pubitemid 44404353)
    • (2005) Reviews of Physiology, Biochemistry and Pharmacology , vol.153 , pp. 1-46
    • Mayer, M.P.1
  • 35
    • 0023511826 scopus 로고
    • Posttranscriptional regulation of hsp70 expression in human cells: Effects of heat shock inhibition of protein synthesis, and adenovirus infection on translation and mRNA stability adenovirus infection on translation and mRNA stability
    • Theodorakis NG, Morimoto RI. Posttranscriptional regulation of hsp70 expression in human cells: effects of heat shock, inhibition of protein synthesis, and adenovirus infection on translation and mRNA stability adenovirus infection on translation and mRNA stability. Mol Cell Biol 1987; 7: 4357-4368.
    • (1987) Mol Cell Biol , vol.7 , pp. 4357-4368
    • Theodorakis, N.G.1    Morimoto, R.I.2
  • 36
    • 0038521274 scopus 로고    scopus 로고
    • Caspase 3 activation is essential for efficient influenza virus propagation
    • DOI 10.1093/emboj/cdg279
    • Wurzer WJ, Planz O, Ehrhardt C, Giner M, Silberzahn T, Pleschka S et al. Caspase 3 activation is essential for efficient influenza virus propagation. EMBO J 2003; 22: 2717-2728. (Pubitemid 36712368)
    • (2003) EMBO Journal , vol.22 , Issue.11 , pp. 2717-2728
    • Wurzer, W.J.1    Planz, O.2    Ehrhardt, C.3    Giner, M.4    Silberzahn, T.5    Pleschka, S.6    Ludwig, S.7
  • 38
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • DOI 10.1093/emboj/20.5.1042
    • Rudiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 2001; 20: 1042-1050. (Pubitemid 32186795)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 39
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the Bid-dependent pathway in tumor necrosis factor-induced apoptosis
    • DOI 10.1128/MCB.22.10.3415-3424.2002
    • Gabai VL, Mabuchi K, Mosser DD, Sherman MY. Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Mol Cell Biol 2002; 22: 3415-3424. (Pubitemid 34453981)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.10 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 40
    • 0035815684 scopus 로고    scopus 로고
    • Influenza Virus-induced AP-1-dependent Gene Expression Requires Activation of the JNK Signaling Pathway
    • DOI 10.1074/jbc.M009902200
    • Ludwig S, Ehrhardt C, Neumeier ER, Kracht M, Rapp UR, Pleschka S. Influenza virusinduced AP-1-dependent gene expression requires activation of the JNK signaling pathway. J Biol Chem 2001; 276: 10990-10998. (Pubitemid 38089279)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10990-10998
    • Ludwig, S.1    Ehrhardt, C.2    Neumeier, E.R.3    Kracht, M.4    Rapp, U.R.5    Pleschka, S.6


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