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Volumn 203, Issue 1, 2013, Pages 115-128

Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin

(20)  Fujita, Naonobu a,b   Morita, Eiji c   Itoh, Takashi f   Tanaka, Atsushi b   Nakaoka, Megumi b   Osada, Yuki a   Umemoto, Tetsuo b   Saitoh, Tatsuya c,d   Nakatogawa, Hitoshi e   Kobayashi, Shouhei g   Haraguchi, Tokuko g   Guan, Jun Lin h   Iwai, Kazuhiro i   Tokunaga, Fuminori j   Saito, Kazunobu c   Ishibashi, Koutaro f   Akira, Shizuo c,d   Fukuda, Mitsunori f   Noda, Takeshi a,b   Yoshimori, Tamotsu a,b  


Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AUTOPHAGY PROTEIN 16L1; CELL PROTEIN; POLYSTYRENE; PROTEIN LC3; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84886897936     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201304188     Document Type: Article
Times cited : (236)

References (45)
  • 1
    • 33745818564 scopus 로고    scopus 로고
    • Autophagy recognizes intracellular Salmonella enterica serovar Typhimurium in damaged vacuoles
    • Birmingham, C.L., and J.H. Brumell. 2006. Autophagy recognizes intracellular Salmonella enterica serovar Typhimurium in damaged vacuoles. Autophagy. 2:156-158.
    • (2006) Autophagy. , vol.2 , pp. 156-158
    • Birmingham, C.L.1    Brumell, J.H.2
  • 2
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • Desjardins, M., L.A. Huber, R.G. Parton, and G. Griffiths. 1994. Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J. Cell Biol. 124:677-688. http://dx.doi.org/10.1083/jcb.124.5.677
    • (1994) J. Cell Biol. , vol.124 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 3
    • 68349143052 scopus 로고    scopus 로고
    • Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy
    • Dupont, N., S. Lacas-Gervais, J. Bertout, I. Paz, B. Freche, G.T. Van Nhieu, F.G. van der Goot, P.J. Sansonetti, and F. Lafont. 2009. Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy. Cell Host Microbe. 6:137-149. http://dx.doi.org/10.1016/j.chom.2009.07.005
    • (2009) Cell Host Microbe. , vol.6 , pp. 137-149
    • Dupont, N.1    Lacas-Gervais, S.2    Bertout, J.3    Paz, I.4    Freche, B.5    Van Nhieu, G.T.6    van der Goot, F.G.7    Sansonetti, P.J.8    Lafont, F.9
  • 4
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspensiongrowing human 293-EBNA1 cells
    • Durocher, Y., S. Perret, and A. Kamen. 2002. High-level and high-throughput recombinant protein production by transient transfection of suspensiongrowing human 293-EBNA1 cells. Nucleic Acids Res. 30:E9. http://dx.doi.org/10.1093/nar/30.2.e9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 5
    • 58149290220 scopus 로고    scopus 로고
    • An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure
    • Fujita, N., M. Hayashi-Nishino, H. Fukumoto, H. Omori, A. Yamamoto, T. Noda, and T. Yoshimori. 2008a. An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure. Mol. Biol. Cell. 19:4651-4659. http://dx.doi.org/10.1091/mbc. E08-03-0312
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 4651-4659
    • Fujita, N.1    Hayashi-Nishino, M.2    Fukumoto, H.3    Omori, H.4    Yamamoto, A.5    Noda, T.6    Yoshimori, T.7
  • 6
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N., T. Itoh, H. Omori, M. Fukuda, T. Noda, and T. Yoshimori. 2008b. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell. 19:2092-2100. http://dx.doi.org/10.1091/mbc. E07-12-1257
    • (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
  • 7
    • 70450248450 scopus 로고    scopus 로고
    • Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: analysis of the organization of the Atg16L1 complex in fibroblasts
    • Fujita, N., T. Saitoh, S. Kageyama, S. Akira, T. Noda, and T. Yoshimori. 2009. Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: analysis of the organization of the Atg16L1 complex in fibroblasts. J. Biol. Chem. 284:32602-32609. http://dx.doi.org/10.1074/jbc. M109.037671
    • (2009) J. Biol. Chem. , vol.284 , pp. 32602-32609
    • Fujita, N.1    Saitoh, T.2    Kageyama, S.3    Akira, S.4    Noda, T.5    Yoshimori, T.6
  • 8
    • 79960735619 scopus 로고    scopus 로고
    • Ubiquitination-mediated autophagy against invading bacteria
    • Fujita, N., and T. Yoshimori. 2011. Ubiquitination-mediated autophagy against invading bacteria. Curr. Opin. Cell Biol. 23:492-497. http://dx.doi.org/10.1016/j.ceb.2011.03.003
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 492-497
    • Fujita, N.1    Yoshimori, T.2
  • 9
    • 58149473435 scopus 로고    scopus 로고
    • Role of ULK-FIP200 complex in mammalian autophagy: FIP200, a counterpart of yeast Atg17?
    • Hara, T., and N. Mizushima. 2009. Role of ULK-FIP200 complex in mammalian autophagy: FIP200, a counterpart of yeast Atg17? Autophagy. 5:85-87. http://dx.doi.org/10.4161/auto.5.1.7180
    • (2009) Autophagy , vol.5 , pp. 85-87
    • Hara, T.1    Mizushima, N.2
  • 10
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R.M., and C.M. Pickart. 1999. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 96:645-653. http://dx.doi.org/10.1016/S0092-8674(00)80575-9
    • (1999) Cell. , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 11
    • 84871006349 scopus 로고    scopus 로고
    • The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for ubiquitin-dependent autophagy of intracellular Salmonella Typhimurium
    • Huett, A., R.J. Heath, J. Begun, S.O. Sassi, L.A. Baxt, J.M. Vyas, M.B. Goldberg, and R.J. Xavier. 2012. The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for ubiquitin-dependent autophagy of intracellular Salmonella Typhimurium. Cell Host Microbe. 12:778-790. http://dx.doi.org/10.1016/j.chom.2012.10.019
    • (2012) Cell Host Microbe. , vol.12 , pp. 778-790
    • Huett, A.1    Heath, R.J.2    Begun, J.3    Sassi, S.O.4    Baxt, L.A.5    Vyas, J.M.6    Goldberg, M.B.7    Xavier, R.J.8
  • 12
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • Itakura, E., and N. Mizushima. 2010. Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy. 6:764-776. http://dx.doi.org/10.4161/auto.6.6.12709
    • (2010) Autophagy. , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 13
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura, E., C. Kishi-Itakura, I. Koyama-Honda, and N. Mizushima. 2012. Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J. Cell Sci. 125:1488-1499. http://dx.doi.org/10.1242/jcs.094110
    • (2012) J. Cell Sci. , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 14
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • Itoh, T., N. Fujita, E. Kanno, A. Yamamoto, T. Yoshimori, and M. Fukuda. 2008. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol. Biol. Cell. 19:2916-2925. http://dx.doi.org/10.1091/mbc. E07-12-1231
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2916-2925
    • Itoh, T.1    Fujita, N.2    Kanno, E.3    Yamamoto, A.4    Yoshimori, T.5    Fukuda, M.6
  • 15
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: a new regulator of NF-kappaB activation
    • Iwai, K., and F. Tokunaga. 2009. Linear polyubiquitination: a new regulator of NF-kappaB activation. EMBO Rep. 10:706-713. http://dx.doi.org/10.1038/embor.2009.144
    • (2009) EMBO Rep. , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 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., H. Omori, T. Saitoh, T. Sone, J.L. Guan, S. Akira, F. Imamoto, T. Noda, and T. Yoshimori. 2011. The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella. Mol. Biol. Cell. 22:2290-2300. http://dx.doi.org/10.1091/mbc. E10-11-0893
    • (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
  • 17
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D.J., M. Babst, and S.D. Emr. 2001. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:145-155. http://dx.doi.org/10.1016/S0092-8674(01)00434-2
    • (2001) Cell. , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 18
    • 59349105233 scopus 로고    scopus 로고
    • Monitoring autophagy in mammalian cultured cells through the dynamics of LC3
    • Kimura, S., N. Fujita, T. Noda, and T. Yoshimori. 2009. Monitoring autophagy in mammalian cultured cells through the dynamics of LC3. Methods Enzymol. 452:1-12. http://dx.doi.org/10.1016/S0076-6879(08)03601-X
    • (2009) Methods Enzymol. , vol.452 , pp. 1-12
    • Kimura, S.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4
  • 23
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • Mizushima, N. 2010. The role of the Atg1/ULK1 complex in autophagy regulation. Curr. Opin. Cell Biol. 22:132-139. http://dx.doi.org/10.1016/j.ceb.2009.12.004
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 24
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • Mizushima, N., A. Kuma, Y. Kobayashi, A. Yamamoto, M. Matsubae, T. Takao, T. Natsume, Y. Ohsumi, and T. Yoshimori. 2003. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J. Cell Sci. 116:1679-1688. http://dx.doi.org/10.1242/jcs.00381
    • (2003) J. Cell Sci. , vol.116 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3    Yamamoto, A.4    Matsubae, M.5    Takao, T.6    Natsume, T.7    Ohsumi, Y.8    Yoshimori, T.9
  • 25
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., B. Levine, A.M. Cuervo, and D.J. Klionsky. 2008. Autophagy fights disease through cellular self-digestion. Nature. 451:1069-1075. http://dx.doi.org/10.1038/nature06639
    • (2008) Nature. , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 26
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: an efficient and stable system for transient packaging of retroviruses
    • Morita, S., T. Kojima, and T. Kitamura. 2000. Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7:1063-1066. http://dx.doi.org/10.1038/sj.gt.3301206
    • (2000) Gene Ther. , vol.7 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 29
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova, N., L. Gakhar, S.C. Winistorfer, L. Yu, S. Ramaswamy, and R.C. Piper. 2010. WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol. Cell. 40:433-443. http://dx.doi.org/10.1016/j.molcel.2010.10.018
    • (2010) Mol. Cell. , vol.40 , pp. 433-443
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5    Piper, R.C.6
  • 31
    • 0141815764 scopus 로고    scopus 로고
    • TWEAK induces NF-kappaB2 p100 processing and long lasting NF-kappaB activation
    • Saitoh, T., M. Nakayama, H. Nakano, H. Yagita, N. Yamamoto, and S. Yamaoka. 2003. TWEAK induces NF-kappaB2 p100 processing and long lasting NF-kappaB activation. J. Biol. Chem. 278:36005-36012. http://dx.doi.org/10.1074/jbc. M304266200
    • (2003) J. Biol. Chem. , vol.278 , pp. 36005-36012
    • Saitoh, T.1    Nakayama, M.2    Nakano, H.3    Yagita, H.4    Yamamoto, N.5    Yamaoka, S.6
  • 35
    • 77950465542 scopus 로고    scopus 로고
    • Current knowledge of the pre-autophagosomal structure (PAS)
    • Suzuki, K., and Y. Ohsumi. 2010. Current knowledge of the pre-autophagosomal structure (PAS). FEBS Lett. 584:1280-1286. http://dx.doi.org/10.1016/j.febslet.2010.02.001
    • (2010) FEBS Lett. , vol.584 , pp. 1280-1286
    • Suzuki, K.1    Ohsumi, Y.2
  • 36
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston, T.L., G. Ryzhakov, S. Bloor, N. von Muhlinen, and F. Randow. 2009. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10:1215-1221. http://dx.doi.org/10.1038/ni.1800
    • (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
  • 37
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston, T.L., M.P. Wandel, N. von Muhlinen, A. Foeglein, and F. Randow. 2012. Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature. 482:414-418. http://dx.doi.org/10.1038/nature10744
    • (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
  • 39
    • 84866300942 scopus 로고    scopus 로고
    • Fluorescencebased sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells
    • van Wijk, S.J., E. Fiskin, M. Putyrski, F. Pampaloni, J. Hou, P. Wild, T. Kensche, H.E. Grecco, P. Bastiaens, and I. Dikic. 2012. Fluorescencebased sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells. Mol. Cell. 47:797-809. http://dx.doi.org/10.1016/j.molcel.2012.06.017
    • (2012) Mol. Cell. , vol.47 , pp. 797-809
    • van Wijk, S.J.1    Fiskin, E.2    Putyrski, M.3    Pampaloni, F.4    Hou, J.5    Wild, P.6    Kensche, T.7    Grecco, H.E.8    Bastiaens, P.9    Dikic, I.10
  • 45
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • Zheng, Y.T., S. Shahnazari, A. Brech, T. Lamark, T. Johansen, and J.H. Brumell. 2009. The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway. J. Immunol. 183:5909-5916. http://dx.doi.org/10.4049/jimmunol.0900441
    • (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


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