메뉴 건너뛰기




Volumn 15, Issue 2, 2014, Pages 239-247

A LC3-interacting motif in the influenza A virus M2 protein is required to subvert autophagy and maintain virion stability

Author keywords

[No Author keywords available]

Indexed keywords

LC3 PROTEIN; PROTEIN M2; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84893969715     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2014.01.006     Document Type: Article
Times cited : (204)

References (59)
  • 1
    • 84869222326 scopus 로고    scopus 로고
    • ATG8 family proteins act as scaffolds for assembly of the ULK complex: Sequence requirements for LC3-interacting region (LIR) motifs
    • E.A. Alemu, T. Lamark, K.M. Torgersen, A.B. Birgisdottir, K.B. Larsen, A. Jain, H. Olsvik, A. ∅vervatn, V. Kirkin, and T. Johansen ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs J. Biol. Chem. 287 2012 39275 39290
    • (2012) J. Biol. Chem. , vol.287 , pp. 39275-39290
    • Alemu, E.A.1    Lamark, T.2    Torgersen, K.M.3    Birgisdottir, A.B.4    Larsen, K.B.5    Jain, A.6    Olsvik, H.7
  • 2
    • 0015898875 scopus 로고
    • Morphogenesis and ultrastructure of respiratory syncytial virus
    • T. Bächi, and C. Howe Morphogenesis and ultrastructure of respiratory syncytial virus J. Virol. 12 1973 1173 1180
    • (1973) J. Virol. , vol.12 , pp. 1173-1180
    • Bächi, T.1    Howe, C.2
  • 5
    • 0037370304 scopus 로고    scopus 로고
    • Reverse genetics studies on the filamentous morphology of influenza A virus
    • S.V. Bourmakina, and A. García-Sastre Reverse genetics studies on the filamentous morphology of influenza A virus J. Gen. Virol. 84 2003 517 527
    • (2003) J. Gen. Virol. , vol.84 , pp. 517-527
    • Bourmakina, S.V.1    García-Sastre, A.2
  • 6
    • 84881552168 scopus 로고    scopus 로고
    • The role of 'eat-me' signals and autophagy cargo receptors in innate immunity
    • K.B. Boyle, and F. Randow The role of 'eat-me' signals and autophagy cargo receptors in innate immunity Curr. Opin. Microbiol. 16 2013 339 348
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 339-348
    • Boyle, K.B.1    Randow, F.2
  • 9
    • 84862888230 scopus 로고    scopus 로고
    • Autophagy: An emerging immunological paradigm
    • V. Deretic Autophagy: an emerging immunological paradigm J. Immunol. 189 2012 15 20
    • (2012) J. Immunol. , vol.189 , pp. 15-20
    • Deretic, V.1
  • 11
    • 1642274781 scopus 로고    scopus 로고
    • The M1 matrix protein controls the filamentous phenotype of influenza A virus
    • C.J. Elleman, and W.S. Barclay The M1 matrix protein controls the filamentous phenotype of influenza A virus Virology 321 2004 144 153
    • (2004) Virology , vol.321 , pp. 144-153
    • Elleman, C.J.1    Barclay, W.S.2
  • 13
    • 84862642115 scopus 로고    scopus 로고
    • Non-canonical translation in RNA viruses
    • A.E. Firth, and I. Brierley Non-canonical translation in RNA viruses J. Gen. Virol. 93 2012 1385 1409
    • (2012) J. Gen. Virol. , vol.93 , pp. 1385-1409
    • Firth, A.E.1    Brierley, I.2
  • 14
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • N. Fujita, T. Itoh, H. Omori, M. Fukuda, T. Noda, and T. Yoshimori The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy Mol. Biol. Cell 19 2008 2092 2100
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 16
    • 75149173978 scopus 로고    scopus 로고
    • Targeting Beclin 1 for viral subversion of macroautophagy
    • M. Gannagé, P.C. Rämer, and C. Münz Targeting Beclin 1 for viral subversion of macroautophagy Autophagy 6 2010 166 167
    • (2010) Autophagy , vol.6 , pp. 166-167
    • Gannagé, M.1    Rämer, P.C.2    Münz, C.3
  • 17
    • 84874724717 scopus 로고    scopus 로고
    • InfluenzaVirus: Here, there, especially air?
    • C.B. Hall InfluenzaVirus: here, there, especially air? J. Infect. Dis. 207 2013 1027 1029
    • (2013) J. Infect. Dis. , vol.207 , pp. 1027-1029
    • Hall, C.B.1
  • 18
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • N.S. Heaton, and G. Randall Dengue virus-induced autophagy regulates lipid metabolism Cell Host Microbe 8 2010 422 432
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 19
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: A structure-function analysis
    • L.J. Holsinger, D. Nichani, L.H. Pinto, and R.A. Lamb Influenza A virus M2 ion channel protein: a structure-function analysis J. Virol. 68 1994 1551 1563
    • (1994) J. Virol. , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 20
    • 56449098772 scopus 로고    scopus 로고
    • Mutational analysis of cis-acting RNA signals in segment 7 of influenza A virus
    • E.C. Hutchinson, M.D. Curran, E.K. Read, J.R. Gog, and P. Digard Mutational analysis of cis-acting RNA signals in segment 7 of influenza A virus J. Virol. 82 2008 11869 11879
    • (2008) J. Virol. , vol.82 , pp. 11869-11879
    • Hutchinson, E.C.1    Curran, M.D.2    Read, E.K.3    Gog, J.R.4    Digard, P.5
  • 23
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • T. Johansen, and T. Lamark Selective autophagy mediated by autophagic adapter proteins Autophagy 7 2011 279 296
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 25
    • 80053302432 scopus 로고    scopus 로고
    • Picornavirus subversion of the autophagy pathway
    • K.A. Klein, and W.T. Jackson Picornavirus subversion of the autophagy pathway Viruses 3 2011 1549 1561
    • (2011) Viruses , vol.3 , pp. 1549-1561
    • Klein, K.A.1    Jackson, W.T.2
  • 26
    • 0021893484 scopus 로고
    • Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface
    • R.A. Lamb, S.L. Zebedee, and C.D. Richardson Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface Cell 40 1985 627 633
    • (1985) Cell , vol.40 , pp. 627-633
    • Lamb, R.A.1    Zebedee, S.L.2    Richardson, C.D.3
  • 28
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: A quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • G.P. Leser, and R.A. Lamb Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins Virology 342 2005 215 227
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 29
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • B. Levine, N. Mizushima, and H.W. Virgin Autophagy in immunity and inflammation Nature 469 2011 323 335
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 30
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • N. Mizushima, and M. Komatsu Autophagy: renovation of cells and tissues Cell 147 2011 728 741
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 31
    • 17444405938 scopus 로고    scopus 로고
    • Mathematical model of influenza A virus production in large-scale microcarrier culture
    • L. Möhler, D. Flockerzi, H. Sann, and U. Reichl Mathematical model of influenza A virus production in large-scale microcarrier culture Biotechnol. Bioeng. 90 2005 46 58
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 46-58
    • Möhler, L.1    Flockerzi, D.2    Sann, H.3    Reichl, U.4
  • 32
    • 84861782476 scopus 로고    scopus 로고
    • Bacterial autophagy: Restriction or promotion of bacterial replication?
    • S. Mostowy, and P. Cossart Bacterial autophagy: restriction or promotion of bacterial replication? Trends Cell Biol. 22 2012 283 291
    • (2012) Trends Cell Biol. , vol.22 , pp. 283-291
    • Mostowy, S.1    Cossart, P.2
  • 33
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • S.L. Noton, E. Medcalf, D. Fisher, A.E. Mullin, D. Elton, and P. Digard Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions J. Gen. Virol. 88 2007 2280 2290
    • (2007) J. Gen. Virol. , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5    Digard, P.6
  • 34
    • 84874382407 scopus 로고    scopus 로고
    • Research funding. A framework for decisions about research with HPAI H5N1 viruses
    • A.P. Patterson, L.A. Tabak, A.S. Fauci, F.S. Collins, and S. Howard Research funding. A framework for decisions about research with HPAI H5N1 viruses Science 339 2013 1036 1037
    • (2013) Science , vol.339 , pp. 1036-1037
    • Patterson, A.P.1    Tabak, L.A.2    Fauci, A.S.3    Collins, F.S.4    Howard, S.5
  • 35
    • 34547408207 scopus 로고    scopus 로고
    • Retroviral transduction of DT40
    • F. Randow, and J.E. Sale Retroviral transduction of DT40 Subcell. Biochem. 40 2006 383 386
    • (2006) Subcell. Biochem. , vol.40 , pp. 383-386
    • Randow, F.1    Sale, J.E.2
  • 36
    • 84877605000 scopus 로고    scopus 로고
    • Cellular self-defense: How cell-autonomous immunity protects against pathogens
    • F. Randow, J.D. MacMicking, and L.C. James Cellular self-defense: how cell-autonomous immunity protects against pathogens Science 340 2013 701 706
    • (2013) Science , vol.340 , pp. 701-706
    • Randow, F.1    Macmicking, J.D.2    James, L.C.3
  • 37
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • B. Ravikumar, K. Moreau, L. Jahreiss, C. Puri, and D.C. Rubinsztein Plasma membrane contributes to the formation of pre-autophagosomal structures Nat. Cell Biol. 12 2010 747 757
    • (2010) Nat. Cell Biol. , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 40
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • J.S. Rossman, and R.A. Lamb Influenza virus assembly and budding Virology 411 2011 229 236
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 41
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus m2 ion channel protein is necessary for filamentous virion formation
    • J.S. Rossman, X. Jing, G.P. Leser, V. Balannik, L.H. Pinto, and R.A. Lamb Influenza virus m2 ion channel protein is necessary for filamentous virion formation J. Virol. 84 2010 5078 5088
    • (2010) J. Virol. , vol.84 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Balannik, V.4    Pinto, L.H.5    Lamb, R.A.6
  • 42
    • 34447342317 scopus 로고    scopus 로고
    • SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK
    • G. Ryzhakov, and F. Randow SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK EMBO J. 26 2007 3180 3190
    • (2007) EMBO J. , vol.26 , pp. 3180-3190
    • Ryzhakov, G.1    Randow, F.2
  • 43
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • J.R. Schnell, and J.J. Chou Structure and mechanism of the M2 proton channel of influenza A virus Nature 451 2008 591 595
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 44
    • 77958156306 scopus 로고    scopus 로고
    • Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer
    • M. Sharma, M. Yi, H. Dong, H. Qin, E. Peterson, D.D. Busath, H.-X. Zhou, and T.A. Cross Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer Science 330 2010 509 512
    • (2010) Science , vol.330 , pp. 509-512
    • Sharma, M.1    Yi, M.2    Dong, H.3    Qin, H.4    Peterson, E.5    Busath, D.D.6    Zhou, H.-X.7    Cross, T.A.8
  • 45
    • 0036401535 scopus 로고    scopus 로고
    • A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions
    • M. Simpson-Holley, D. Ellis, D. Fisher, D. Elton, J. McCauley, and P. Digard A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions Virology 301 2002 212 225
    • (2002) Virology , vol.301 , pp. 212-225
    • Simpson-Holley, M.1    Ellis, D.2    Fisher, D.3    Elton, D.4    McCauley, J.5    Digard, P.6
  • 48
    • 80053964069 scopus 로고    scopus 로고
    • Ultracentrifugation deforms unfixed influenza A virions
    • Y. Sugita, T. Noda, H. Sagara, and Y. Kawaoka Ultracentrifugation deforms unfixed influenza A virions J. Gen. Virol. 92 2011 2485 2493
    • (2011) J. Gen. Virol. , vol.92 , pp. 2485-2493
    • Sugita, Y.1    Noda, T.2    Sagara, H.3    Kawaoka, Y.4
  • 49
    • 77956499048 scopus 로고    scopus 로고
    • Influenza virus evolution, host adaptation, and pandemic formation
    • J.K. Taubenberger, and J.C. Kash Influenza virus evolution, host adaptation, and pandemic formation Cell Host Microbe 7 2010 440 451
    • (2010) Cell Host Microbe , vol.7 , pp. 440-451
    • Taubenberger, J.K.1    Kash, J.C.2
  • 50
    • 0024282829 scopus 로고
    • Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and v of the paramyxovirus SV5
    • S.M. Thomas, R.A. Lamb, and R.G. Paterson Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the paramyxovirus SV5 Cell 54 1988 891 902
    • (1988) Cell , vol.54 , pp. 891-902
    • Thomas, S.M.1    Lamb, R.A.2    Paterson, R.G.3
  • 51
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • T.L.M. Thurston, G. Ryzhakov, S. Bloor, N. von Muhlinen, and F. Randow The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria Nat. Immunol. 10 2009 1215 1221
    • (2009) Nat. Immunol. , vol.10 , pp. 1215-1221
    • Thurston, T.L.M.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 52
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • T.L.M. Thurston, M.P. Wandel, N. von Muhlinen, A. Foeglein, and F. Randow Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion Nature 482 2012 414 418
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.M.1    Wandel, M.P.2    Von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 53
    • 31344475650 scopus 로고
    • The influenza virus: Its morphology, immunology, and kinetics of multiplication
    • P. von Magnus The influenza virus: its morphology, immunology, and kinetics of multiplication Bull. World Health Organ. 8 1953 647 660
    • (1953) Bull. World Health Organ. , vol.8 , pp. 647-660
    • Von Magnus, P.1
  • 58
    • 0034093648 scopus 로고    scopus 로고
    • Filamentous particle formation by human parainfluenza virus type 2
    • Q. Yao, and R.W. Compans Filamentous particle formation by human parainfluenza virus type 2 J. Gen. Virol. 81 2000 1305 1312
    • (2000) J. Gen. Virol. , vol.81 , pp. 1305-1312
    • Yao, Q.1    Compans, R.W.2
  • 59
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • Y.T. Zheng, S. Shahnazari, A. Brech, T. Lamark, T. Johansen, and J.H. Brumell The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway J. Immunol. 183 2009 5909 5916
    • (2009) J. Immunol. , vol.183 , pp. 5909-5916
    • Zheng, Y.T.1    Shahnazari, S.2    Brech, A.3    Lamark, T.4    Johansen, T.5    Brumell, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.