메뉴 건너뛰기




Volumn 287, Issue 16, 2012, Pages 12668-12678

Mycobacterial induction of autophagy varies by species and occurs independently of mammalian target of rapamycin inhibition

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY; BACTERIAL VIABILITY; HOST CELLS; INHIBITORY MECHANISM; MAMMALIAN AUTOPHAGY; MAMMALIAN TARGET; MAMMALIAN TARGET OF RAPAMYCIN (MTOR); MTOR SIGNALING; MULTIPLE FACTORS; MYCOBACTERIAL; MYCOBACTERIAL INFECTION; MYCOBACTERIUM BOVIS; MYCOBACTERIUM SMEGMATIS; RAPAMYCIN TREATMENT;

EID: 84859779956     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.320135     Document Type: Article
Times cited : (74)

References (36)
  • 1
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C., and Klionsky, D. J. (2009) Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 2
    • 0037097863 scopus 로고    scopus 로고
    • Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
    • DOI 10.1101/gad.995802
    • Fingar, D. C., Salama, S., Tsou, C., Harlow, E., and Blenis, J. (2002) Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. Genes Dev. 16, 1472-1487 (Pubitemid 34686329)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1472-1487
    • Fingar, D.C.1    Salama, S.2    Tsou, C.3    Harlow, E.4    Blenis, J.5
  • 3
    • 78651284554 scopus 로고    scopus 로고
    • The complexes of mammalian target of rapamycin
    • Zhou, H., and Huang, S. (2010) The complexes of mammalian target of rapamycin. Curr. Protein Pept. Sci. 11, 409-424
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 409-424
    • Zhou, H.1    Huang, S.2
  • 4
    • 79951910694 scopus 로고    scopus 로고
    • Autophagy in immunity and cell-autonomous defense against intracellular microbes
    • Deretic, V. (2011) Autophagy in immunity and cell-autonomous defense against intracellular microbes. Immunol. Rev. 240, 92-104
    • (2011) Immunol. Rev. , vol.240 , pp. 92-104
    • Deretic, V.1
  • 6
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • DOI 10.1016/j.cell.2004.11.038, PII S0092867404011067
    • Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I., and Deretic, V. (2004) Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753-766 (Pubitemid 40017683)
    • (2004) Cell , vol.119 , Issue.6 , 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
  • 7
    • 77649112187 scopus 로고    scopus 로고
    • Genome-wide analysis of the host intracellular network that regulates survival of Mycobacterium tuberculosis
    • Kumar, D., Nath, L., Kamal, M. A., Varshney, A., Jain, A., Singh, S., and Rao, K. V. (2010) Genome-wide analysis of the host intracellular network that regulates survival of Mycobacterium tuberculosis. Cell 140, 731-743
    • (2010) Cell , vol.140 , pp. 731-743
    • Kumar, D.1    Nath, L.2    Kamal, M.A.3    Varshney, A.4    Jain, A.5    Singh, S.6    Rao, K.V.7
  • 9
    • 79952333943 scopus 로고    scopus 로고
    • Autophagy and p62/sequestosome 1 generate neo-antimicrobial peptides (cryptides) from cytosolic proteins
    • Ponpuak, M., and Deretic, V. (2011) Autophagy and p62/sequestosome 1 generate neo-antimicrobial peptides (cryptides) from cytosolic proteins. Autophagy 7, 336-337
    • (2011) Autophagy , vol.7 , pp. 336-337
    • Ponpuak, M.1    Deretic, V.2
  • 11
    • 77955146917 scopus 로고    scopus 로고
    • Autophagy and adaptive immunity
    • Crotzer, V. L., and Blum, J. S. (2010) Autophagy and adaptive immunity. Immunology 131, 9-17
    • (2010) Immunology , vol.131 , pp. 9-17
    • Crotzer, V.L.1    Blum, J.S.2
  • 12
    • 62049084947 scopus 로고    scopus 로고
    • Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells
    • Jagannath, C., Lindsey, D. R., Dhandayuthapani, S., Xu, Y., Hunter, R. L., Jr., and Eissa, N. T. (2009) Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells. Nat. Med. 15, 267-276
    • (2009) Nat. Med. , vol.15 , pp. 267-276
    • Jagannath, C.1    Lindsey, D.R.2    Dhandayuthapani, S.3    Xu, Y.4    Hunter Jr., R.L.5    Eissa, N.T.6
  • 13
    • 79955961624 scopus 로고    scopus 로고
    • Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system
    • Lerena, M. C., and Colombo, M. I. (2011) Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system. Cell Microbiol. 13, 814-835
    • (2011) Cell Microbiol. , vol.13 , pp. 814-835
    • Lerena, M.C.1    Colombo, M.I.2
  • 14
    • 77952718880 scopus 로고    scopus 로고
    • Survival mechanisms of pathogenic Mycobacterium tuberculosis H37Rv
    • Meena, L. S., and Rajni (2010) Survival mechanisms of pathogenic Mycobacterium tuberculosis H37Rv. FEBS J. 277, 2416-2427
    • (2010) FEBS J. , vol.277 , pp. 2416-2427
    • Meena, L.S.1    Rajni2
  • 16
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T., and Jacobs, W. R., Jr. (1990) Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4, 1911-1919
    • (1990) Mol. Microbiol. , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs Jr., W.R.5
  • 18
    • 66449114447 scopus 로고    scopus 로고
    • Identification of the small protein rich in arginine and glycine (SRAG). A newly identified nucleolar protein that can regulate cell proliferation
    • Zullo, A. J., Michaud, M., Zhang, W., and Grusby, M. J. (2009) Identification of the small protein rich in arginine and glycine (SRAG). A newly identified nucleolar protein that can regulate cell proliferation. J. Biol. Chem. 284, 12504-12511
    • (2009) J. Biol. Chem. , vol.284 , pp. 12504-12511
    • Zullo, A.J.1    Michaud, M.2    Zhang, W.3    Grusby, M.J.4
  • 19
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • Kimura, S., Noda, T., and Yoshimori, T. (2007) Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent- tagged LC3. Autophagy 3, 452-460 (Pubitemid 47293726)
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 21
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • DOI 10.1038/ncb1740, PII NCB1740
    • Liang, C., Lee, J. S., Inn, K. S., Gack, M. U., Li, Q., Roberts, E. A., Vergne, I., Deretic, V., Feng, P., Akazawa, C., and Jung, J. U. (2008) Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat. Cell Biol. 10, 776-787 (Pubitemid 351927707)
    • (2008) Nature Cell Biology , vol.10 , Issue.7 , pp. 776-787
    • Liang, C.1    Lee, J.-S.2    Inn, K.-S.3    Gack, M.U.4    Li, Q.5    Roberts, E.A.6    Vergne, I.7    Deretic, V.8    Feng, P.9    Akazawa, C.10    Jung, J.U.11
  • 22
    • 76249108700 scopus 로고    scopus 로고
    • Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm
    • Ha, S. D., Ham, B., Mogridge, J., Saftig, P., Lin, S., and Kim, S. O. (2010) Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm. J. Biol. Chem. 285, 2120-2129
    • (2010) J. Biol. Chem. , vol.285 , pp. 2120-2129
    • Ha, S.D.1    Ham, B.2    Mogridge, J.3    Saftig, P.4    Lin, S.5    Kim, S.O.6
  • 24
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy. Assays and artifacts
    • Barth, S., Glick, D., and Macleod, K. F. (2010) Autophagy. Assays and artifacts. J. Pathol. 221, 117-124
    • (2010) J. Pathol. , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    Macleod, K.F.3
  • 27
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblotting
    • Mizushima, N., and Yoshimori, T. (2007) How to interpret LC3 immunoblotting. Autophagy 3, 542-545 (Pubitemid 350060049)
    • (2007) Autophagy , vol.3 , Issue.6 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 28
    • 77955708390 scopus 로고    scopus 로고
    • Overview of macroautophagy regulation in mammalian cells
    • Mehrpour, M., Esclatine, A., Beau, I., and Codogno, P. (2010) Overview of macroautophagy regulation in mammalian cells. Cell Res. 20, 748-762
    • (2010) Cell Res. , vol.20 , pp. 748-762
    • Mehrpour, M.1    Esclatine, A.2    Beau, I.3    Codogno, P.4
  • 29
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive. A history of macroautophagy
    • Yang, Z., and Klionsky, D. J. (2010) Eaten alive. A history of macroautophagy. Nat. Cell Biol. 12, 814-822
    • (2010) Nat. Cell Biol. , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 30
    • 80051813164 scopus 로고    scopus 로고
    • Eating the strangers within. Host control of intracellular bacteria via xenophagy
    • Knodler, L. A., and Celli, J. (2011) Eating the strangers within. Host control of intracellular bacteria via xenophagy. Cell Microbiol. 13, 1319-1327
    • (2011) Cell Microbiol. , vol.13 , pp. 1319-1327
    • Knodler, L.A.1    Celli, J.2
  • 31
    • 79961122410 scopus 로고    scopus 로고
    • Regulation of autophagy by lysosomal positioning
    • Korolchuk, V. I., and Rubinsztein, D. C. (2011) Regulation of autophagy by lysosomal positioning. Autophagy 7, 927-928
    • (2011) Autophagy , vol.7 , pp. 927-928
    • Korolchuk, V.I.1    Rubinsztein, D.C.2
  • 32
    • 59449103030 scopus 로고    scopus 로고
    • Host cell autophagy is induced by Toxoplasma gondii and contributes to parasite growth
    • Wang, Y., Weiss, L. M., and Orlofsky, A. (2009) Host cell autophagy is induced by Toxoplasma gondii and contributes to parasite growth. J. Biol. Chem. 284, 1694-1701
    • (2009) J. Biol. Chem. , vol.284 , pp. 1694-1701
    • Wang, Y.1    Weiss, L.M.2    Orlofsky, A.3
  • 34
    • 65349123115 scopus 로고    scopus 로고
    • Interaction of Mycobacterium tuberculosis with the host. Consequences for vaccine development
    • Dietrich, J., and Doherty, T. M. (2009) Interaction of Mycobacterium tuberculosis with the host. Consequences for vaccine development. APMIS 117, 440-457
    • (2009) APMIS , vol.117 , pp. 440-457
    • Dietrich, J.1    Doherty, T.M.2
  • 35
    • 0032534586 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase, protein kinase B, and p70 S6 kinases in lipopolysaccharide-stimulated raw 264.7 cells: Differential effects of rapamycin, Ly294002, and wortmannin on nitric oxide production
    • Salh, B., Wagey, R., Marotta, A., Tao, J. S., and Pelech, S. (1998) Activation of phosphatidylinositol 3-kinase, protein kinase B, and p70 S6 kinases in lipopolysaccharide-stimulated Raw 264.7 cells. Differential effects of rapamycin, Ly294002, and wortmannin on nitric oxide production. J. Immunol. 161, 6947-6954 (Pubitemid 28562242)
    • (1998) Journal of Immunology , vol.161 , Issue.12 , pp. 6947-6954
    • Salh, B.1    Wagey, R.2    Marotta, A.3    Tao, J.S.4    Pelech, S.5
  • 36
    • 0030070034 scopus 로고    scopus 로고
    • Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species
    • Ortalo-Magné, A., Lemassu, A., Lanéelle, M. A., Bardou, F., Silve, G., Gounon, P., Marchal, G., and Daffé, M. (1996) Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species. J. Bacteriol. 178, 456-461
    • (1996) J. Bacteriol. , vol.178 , pp. 456-461
    • Ortalo-Magné, A.1    Lemassu, A.2    Lanéelle, M.A.3    Bardou, F.4    Silve, G.5    Gounon, P.6    Marchal, G.7    Daffé, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.