메뉴 건너뛰기




Volumn 22, Issue 13, 2012, Pages R540-R545

Interactions of Pathogenic Bacteria with Autophagy Systems

Author keywords

[No Author keywords available]

Indexed keywords

ATG5 PROTEIN, HUMAN; BACTERIAL TOXIN; LIGHT CHAIN 3, HUMAN; MICROTUBULE ASSOCIATED PROTEIN;

EID: 84872113974     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2012.06.001     Document Type: Review
Times cited : (139)

References (50)
  • 1
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • Yang, Z., Klionsky, D.J., Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22 (2010), 124–131.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 3
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic, V., Levine, B., Autophagy, immunity, and microbial adaptations. Cell Host Microbe 5 (2009), 527–549.
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 7
    • 79952613917 scopus 로고    scopus 로고
    • The Burkholderia pseudomallei type III secretion system and BopA are required for evasion of LC3-associated phagocytosis
    • Gong, L., Cullinane, M., Treerat, P., Ramm, G., Prescott, M., Adler, B., Boyce, J.D., Devenish, R.J., The Burkholderia pseudomallei type III secretion system and BopA are required for evasion of LC3-associated phagocytosis. PLoS One, 6, 2011, e17852.
    • (2011) PLoS One , vol.6 , pp. e17852
    • Gong, L.1    Cullinane, M.2    Treerat, P.3    Ramm, G.4    Prescott, M.5    Adler, B.6    Boyce, J.D.7    Devenish, R.J.8
  • 9
    • 80054825045 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells
    • Martinez, J., Almendinger, J., Oberst, A., Ness, R., Dillon, C.P., Fitzgerald, P., Hengartner, M.O., Green, D.R., Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells. Proc. Natl. Acad. Sci. USA 108 (2011), 17396–17401.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 17396-17401
    • Martinez, J.1    Almendinger, J.2    Oberst, A.3    Ness, R.4    Dillon, C.P.5    Fitzgerald, P.6    Hengartner, M.O.7    Green, D.R.8
  • 11
    • 80455122654 scopus 로고    scopus 로고
    • Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes
    • Florey, O., Kim, S.E., Sandoval, C.P., Haynes, C.M., Overholtzer, M., Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes. Nat. Cell Biol. 13 (2011), 1335–1343.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1335-1343
    • Florey, O.1    Kim, S.E.2    Sandoval, C.P.3    Haynes, C.M.4    Overholtzer, M.5
  • 12
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • Gutierrez, M.G., Master, S.S., Singh, S.B., Taylor, G.A., Colombo, M.I., Deretic, V., Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119 (2004), 753–766.
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 13
    • 34250802980 scopus 로고    scopus 로고
    • Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy
    • Alonso, S., Pethe, K., Russell, D.G., Purdy, G.E., Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy. Proc. Natl. Acad. Sci. USA 104 (2007), 6031–6036.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6031-6036
    • Alonso, S.1    Pethe, K.2    Russell, D.G.3    Purdy, G.E.4
  • 14
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • Birmingham, C.L., Smith, A.C., Bakowski, M.A., Yoshimori, T., Brumell, J.H., Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J. Biol. Chem. 281 (2006), 11374–11383.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11374-11383
    • Birmingham, C.L.1    Smith, A.C.2    Bakowski, M.A.3    Yoshimori, T.4    Brumell, J.H.5
  • 15
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • Zheng, Y.T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., Brumell, J.H., 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
  • 16
    • 79959874238 scopus 로고    scopus 로고
    • The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella
    • Kageyama, S., Omori, H., Saitoh, T., Sone, T., Guan, J.L., Akira, S., Imamoto, F., Noda, T., Yoshimori, T., The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella. Mol. Biol. Cell 22 (2011), 2290–2300.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2290-2300
    • Kageyama, S.1    Omori, H.2    Saitoh, T.3    Sone, T.4    Guan, J.L.5    Akira, S.6    Imamoto, F.7    Noda, T.8    Yoshimori, T.9
  • 22
    • 2342464290 scopus 로고    scopus 로고
    • Recognition of bacteria in the cytosol of Mammalian cells by the ubiquitin system
    • Perrin, A.J., Jiang, X., Birmingham, C.L., So, N.S., Brumell, J.H., Recognition of bacteria in the cytosol of Mammalian cells by the ubiquitin system. Curr. Biol. 14 (2004), 806–811.
    • (2004) Curr. Biol. , vol.14 , pp. 806-811
    • Perrin, A.J.1    Jiang, X.2    Birmingham, C.L.3    So, N.S.4    Brumell, J.H.5
  • 26
    • 0031930276 scopus 로고    scopus 로고
    • Chronic Listeria infection in SCID mice: requirements for the carrier state and the dual role of T cells in transferring protection or suppression
    • Bhardwaj, V., Kanagawa, O., Swanson, P.E., Unanue, E.R., Chronic Listeria infection in SCID mice: requirements for the carrier state and the dual role of T cells in transferring protection or suppression. J. Immunol. 160 (1998), 376–384.
    • (1998) J. Immunol. , vol.160 , pp. 376-384
    • Bhardwaj, V.1    Kanagawa, O.2    Swanson, P.E.3    Unanue, E.R.4
  • 27
    • 33645553471 scopus 로고    scopus 로고
    • Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles
    • Shaughnessy, L.M., Hoppe, A.D., Christensen, K.A., Swanson, J.A., Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles. Cell Microbiol. 8 (2006), 781–792.
    • (2006) Cell Microbiol. , vol.8 , pp. 781-792
    • Shaughnessy, L.M.1    Hoppe, A.D.2    Christensen, K.A.3    Swanson, J.A.4
  • 29
    • 66549126665 scopus 로고    scopus 로고
    • Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification
    • Pujol, C., Klein, K.A., Romanov, G.A., Palmer, L.E., Cirota, C., Zhao, Z., Bliska, J.B., Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification. Infect. Immun. 77 (2009), 2251–2261.
    • (2009) Infect. Immun. , vol.77 , pp. 2251-2261
    • Pujol, C.1    Klein, K.A.2    Romanov, G.A.3    Palmer, L.E.4    Cirota, C.5    Zhao, Z.6    Bliska, J.B.7
  • 30
    • 38849200959 scopus 로고    scopus 로고
    • Subversion of cellular autophagy by Anaplasma phagocytophilum
    • Niu, H., Yamaguchi, M., Rikihisa, Y., Subversion of cellular autophagy by Anaplasma phagocytophilum. Cell Microbiol. 10 (2008), 593–605.
    • (2008) Cell Microbiol. , vol.10 , pp. 593-605
    • Niu, H.1    Yamaguchi, M.2    Rikihisa, Y.3
  • 31
    • 34047271297 scopus 로고    scopus 로고
    • Staphylococcus aureus subvert autophagy for induction of caspase-independent host cell death
    • Schnaith, A., Kashkar, H., Leggio, S.A., Addicks, K., Kronke, M., Krut, O., Staphylococcus aureus subvert autophagy for induction of caspase-independent host cell death. J. Biol. Chem. 282 (2007), 2695–2706.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2695-2706
    • Schnaith, A.1    Kashkar, H.2    Leggio, S.A.3    Addicks, K.4    Kronke, M.5    Krut, O.6
  • 32
    • 76749117962 scopus 로고    scopus 로고
    • Coxiella burnetii modulates Beclin 1 and Bcl-2, preventing host cell apoptosis to generate a persistent bacterial infection
    • Vazquez, C.L., Colombo, M.I., Coxiella burnetii modulates Beclin 1 and Bcl-2, preventing host cell apoptosis to generate a persistent bacterial infection. Cell Death Differ. 17 (2010), 421–438.
    • (2010) Cell Death Differ. , vol.17 , pp. 421-438
    • Vazquez, C.L.1    Colombo, M.I.2
  • 33
    • 19644382161 scopus 로고    scopus 로고
    • Autophagy is an immediate macrophage response to Legionella pneumophila
    • Amer, A.O., Swanson, M.S., Autophagy is an immediate macrophage response to Legionella pneumophila. Cell Microbiol. 7 (2005), 765–778.
    • (2005) Cell Microbiol. , vol.7 , pp. 765-778
    • Amer, A.O.1    Swanson, M.S.2
  • 34
    • 0034613726 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles
    • Sturgill-Koszycki, S., Swanson, M.S., Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles. J. Exp. Med. 192 (2000), 1261–1272.
    • (2000) J. Exp. Med. , vol.192 , pp. 1261-1272
    • Sturgill-Koszycki, S.1    Swanson, M.S.2
  • 35
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication
    • Checroun, C., Wehrly, T.D., Fischer, E.R., Hayes, S.F., Celli, J., Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc. Natl. Acad. Sci. USA 103 (2006), 14578–14583.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14578-14583
    • Checroun, C.1    Wehrly, T.D.2    Fischer, E.R.3    Hayes, S.F.4    Celli, J.5
  • 36
    • 79960735619 scopus 로고    scopus 로고
    • Ubiquitination-mediated autophagy against invading bacteria
    • Fujita, N., Yoshimori, T., Ubiquitination-mediated autophagy against invading bacteria. Curr. Opin. Cell Biol. 23 (2011), 492–497.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 492-497
    • Fujita, N.1    Yoshimori, T.2
  • 37
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston, T.L., Ryzhakov, G., Bloor, S., von Muhlinen, N., Randow, F., 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.1    Ryzhakov, G.2    Bloor, S.3    von Muhlinen, N.4    Randow, F.5
  • 38
    • 79952348751 scopus 로고    scopus 로고
    • The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway
    • Cemma, M., Kim, P.K., Brumell, J.H., The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway. Autophagy 7 (2011), 341–345.
    • (2011) Autophagy , vol.7 , pp. 341-345
    • Cemma, M.1    Kim, P.K.2    Brumell, J.H.3
  • 40
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston, T.L., Wandel, M.P., von Muhlinen, N., Foeglein, A., Randow, F., 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.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 46
    • 80052385974 scopus 로고    scopus 로고
    • Bacterial toxins can inhibit host cell autophagy through cAMP generation
    • Shahnazari, S., Namolovan, A., Mogridge, J., Kim, P.K., Brumell, J.H., Bacterial toxins can inhibit host cell autophagy through cAMP generation. Autophagy 7 (2011), 957–965.
    • (2011) Autophagy , vol.7 , pp. 957-965
    • Shahnazari, S.1    Namolovan, A.2    Mogridge, J.3    Kim, P.K.4    Brumell, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.