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Volumn 4, Issue SEP, 2013, Pages

Intestinal epithelium and autophagy: Partners in gut homeostasis

Author keywords

ATG16L1; Autophagy; IBD; Intestinal epithelium; IRGM

Indexed keywords

ATG16L1 PROTEIN; AUTOPHAGY PROTEIN 5; BECLIN 1; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; ESCRT PROTEIN; GAMMA INTERFERON; INTERLEUKIN 1BETA; INTERLEUKIN 6; IRGM PROTEIN; LEUCINE RICH REPEAT KINASE 2; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MICRORNA; MICRORNA 196; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 2; PEPTIDES AND PROTEINS; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P62; PROTEIN SERINE THREONINE KINASE VPS15; RAB7 PROTEIN; SNARE PROTEIN; STAT1 PROTEIN; STAT3 PROTEIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; ULK1 PROTEIN; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 84885998575     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00301     Document Type: Review
Times cited : (98)

References (119)
  • 1
    • 84869498101 scopus 로고    scopus 로고
    • Chaperones in autophagy
    • doi: 10.1016/j.phrs.2012.10.002
    • Kaushik S, Cuervo AM. Chaperones in autophagy. Pharmacol Res (2012) 66(6):484-93. doi: 10.1016/j.phrs.2012.10.002.
    • (2012) Pharmacol Res , vol.66 , Issue.6 , pp. 484-493
    • Kaushik, S.1    Cuervo, A.M.2
  • 2
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: revisiting a 40-year-old conundrum
    • doi:10.4161/auto.7.7.14733
    • Mijaljica D, Prescott M, Devenish RJ. Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy (2011) 7(7):673-82. doi:10.4161/auto.7.7.14733.
    • (2011) Autophagy , vol.7 , Issue.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 3
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • doi:10.1038/nature03029
    • Kuma A, Hatano M, Matsui M, Yamamoto A, Nakaya H, Yoshimori T, et al. The role of autophagy during the early neonatal starvation period. Nature (2004) 432(7020):1032-6. doi:10.1038/nature03029.
    • (2004) Nature , vol.432 , Issue.7020 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 4
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • doi:10.1083/jcb.200412022
    • Komatsu M, Waguri S, Ueno T, Iwata J, Murata S, Tanida I, et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J Cell Biol (2005) 169(3):425-34. doi:10.1083/jcb.200412022.
    • (2005) J Cell Biol , vol.169 , Issue.3 , pp. 425-434
    • Komatsu, M.1    Waguri, S.2    Ueno, T.3    Iwata, J.4    Murata, S.5    Tanida, I.6
  • 5
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • doi:10.1128/MCB.01453-06
    • Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol (2006) 26(24):9220-31. doi:10.1128/MCB.01453-06.
    • (2006) Mol Cell Biol , vol.26 , Issue.24 , pp. 9220-9231
    • Ogata, M.1    Hino, S.2    Saito, A.3    Morikawa, K.4    Kondo, S.5    Kanemoto, S.6
  • 6
    • 34249934085 scopus 로고    scopus 로고
    • Selective degradation of mitochondria by mitophagy
    • doi:10.1016/j.abb.2007.03.034
    • Kim I, Rodriguez-Enriquez S, Lemasters JJ. Selective degradation of mitochondria by mitophagy. Arch Biochem Biophys (2007) 462(2):245-53. doi:10.1016/j.abb.2007.03.034.
    • (2007) Arch Biochem Biophys , vol.462 , Issue.2 , pp. 245-253
    • Kim, I.1    Rodriguez-Enriquez, S.2    Lemasters, J.J.3
  • 7
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • doi:10.1038/ncb1723
    • Kraft C, Deplazes A, Sohrmann M, Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol (2008) 10(5):602-10. doi:10.1038/ncb1723.
    • (2008) Nat Cell Biol , vol.10 , Issue.5 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 8
    • 0033490110 scopus 로고    scopus 로고
    • Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway
    • Hutchins MU, Veenhuis M, Klionsky DJ. Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway. J Cell Sci (1999) 112(Pt 22):4079-87.
    • (1999) J Cell Sci , vol.112 , Issue.PART 22 , pp. 4079-4087
    • Hutchins, M.U.1    Veenhuis, M.2    Klionsky, D.J.3
  • 9
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • doi:10.1371/journal.pbio.0040423
    • Bernales S, McDonald KL, Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol (2006) 4(12):e423. doi:10.1371/journal.pbio.0040423.
    • (2006) PLoS Biol , vol.4 , Issue.12
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 10
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • doi:10.1038/nature09782
    • Levine B, Mizushima N, Virgin HW. Autophagy in immunity and inflammation. Nature (2011) 469(7330):323-35. doi:10.1038/nature09782.
    • (2011) Nature , vol.469 , Issue.7330 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 11
    • 0014148066 scopus 로고
    • Participation of lysosomes in cellular autophagy induced in rat liver by glucagon
    • doi:10.1083/jcb.35.2.C11
    • Deter RL, Baudhuin P, De Duve C. Participation of lysosomes in cellular autophagy induced in rat liver by glucagon. J Cell Biol (1967) 35(2):C11-6. doi:10.1083/jcb.35.2.C11.
    • (1967) J Cell Biol , vol.35 , Issue.2
    • Deter, R.L.1    Baudhuin, P.2    De Duve, C.3
  • 12
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • doi:10.1016/0014-5793(93)80398-E
    • Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett (1993) 333(1-2):169-74. doi:10.1016/0014-5793(93)80398-E.
    • (1993) FEBS Lett , vol.333 , Issue.1-2 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 13
    • 41749114288 scopus 로고    scopus 로고
    • Autophagy: basic principles and relevance to disease
    • doi:10.1146/annurev.pathmechdis.2.010506.091842
    • Kundu M, Thompson CB. Autophagy: basic principles and relevance to disease. Annu Rev Pathol (2008) 3:427-55. doi:10.1146/annurev.pathmechdis.2.010506.091842.
    • (2008) Annu Rev Pathol , vol.3 , pp. 427-455
    • Kundu, M.1    Thompson, C.B.2
  • 14
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • doi:10.1146/annurev-biochem-052709-094552
    • Weidberg H, Shvets E, Elazar Z. Biogenesis and cargo selectivity of autophagosomes. Annu Rev Biochem (2011) 80:125-56. doi:10.1146/annurev-biochem-052709-094552.
    • (2011) Annu Rev Biochem , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 15
    • 78149475088 scopus 로고    scopus 로고
    • Regulation of mammalian autophagy in physiology and pathophysiology
    • doi:10.1152/physrev.00030.2009
    • Ravikumar B, Sarkar S, Davies JE, Futter M, Garcia-Arencibia M, Green-Thompson ZW, et al. Regulation of mammalian autophagy in physiology and pathophysiology. Physiol Rev (2010) 90(4):1383-435. doi:10.1152/physrev.00030.2009.
    • (2010) Physiol Rev , vol.90 , Issue.4 , pp. 1383-1435
    • Ravikumar, B.1    Sarkar, S.2    Davies, J.E.3    Futter, M.4    Garcia-Arencibia, M.5    Green-Thompson, Z.W.6
  • 16
    • 74949090299 scopus 로고    scopus 로고
    • An overview of the molecular mechanism of autophagy
    • doi:10.1007/978-3-642-00302-8_1
    • Yang Z, Klionsky DJ. An overview of the molecular mechanism of autophagy. Curr Top Microbiol Immunol (2009) 335:1-32. doi:10.1007/978-3-642-00302-8_1.
    • (2009) Curr Top Microbiol Immunol , vol.335 , pp. 1-32
    • Yang, Z.1    Klionsky, D.J.2
  • 17
    • 84859779956 scopus 로고    scopus 로고
    • Mycobacterial induction of autophagy varies by species and occurs independently of mammalian target of rapamycin inhibition
    • doi:10.1074/jbc. M111.320135
    • Zullo AJ, Lee S. Mycobacterial induction of autophagy varies by species and occurs independently of mammalian target of rapamycin inhibition. J Biol Chem (2012) 287(16):12668-78. doi:10.1074/jbc. M111.320135.
    • (2012) J Biol Chem , vol.287 , Issue.16 , pp. 12668-78
    • Zullo, A.J.1    Lee, S.2
  • 18
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • doi:10.1083/jcb.200712064
    • Hara T, Takamura A, Kishi C, Iemura S, Natsume T, Guan JL, et al. FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J Cell Biol (2008) 181(3):497-510. doi:10.1083/jcb.200712064.
    • (2008) J Cell Biol , vol.181 , Issue.3 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3    Iemura, S.4    Natsume, T.5    Guan, J.L.6
  • 19
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • doi:10.1038/ncb2152
    • Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol (2011) 13(2):132-41. doi:10.1038/ncb2152.
    • (2011) Nat Cell Biol , vol.13 , Issue.2 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 20
    • 67549110195 scopus 로고    scopus 로고
    • A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy
    • doi:10.4161/auto.5.5.8249
    • Mercer CA, Kaliappan A, Dennis PB. A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy. Autophagy (2009) 5(5):649-62. doi:10.4161/auto.5.5.8249.
    • (2009) Autophagy , vol.5 , Issue.5 , pp. 649-662
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 21
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • doi:10.1091/mbc. E08-12-1249
    • Jung CH, Jun CB, Ro SH, Kim YM, Otto NM, Cao J, et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell (2009) 20(7):1992-2003. doi:10.1091/mbc. E08-12-1249.
    • (2009) Mol Biol Cell , vol.20 , Issue.7 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6
  • 22
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
    • doi:10.1091/mbc. E08-12-1248
    • Hosokawa N, Hara T, Kaizuka T, Kishi C, Takamura A, Miura Y, et al. Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. Mol Biol Cell (2009) 20(7):1981-91. doi:10.1091/mbc. E08-12-1248.
    • (2009) Mol Biol Cell , vol.20 , Issue.7 , pp. 1981-1991
    • Hosokawa, N.1    Hara, T.2    Kaizuka, T.3    Kishi, C.4    Takamura, A.5    Miura, Y.6
  • 23
    • 82855170846 scopus 로고    scopus 로고
    • Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction
    • doi:10.4161/auto.7.12.18027
    • Alers S, Loffler AS, Paasch F, Dieterle AM, Keppeler H, Lauber K, et al. Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction. Autophagy (2011) 7(12):1423-33. doi:10.4161/auto.7.12.18027.
    • (2011) Autophagy , vol.7 , Issue.12 , pp. 1423-1433
    • Alers, S.1    Loffler, A.S.2    Paasch, F.3    Dieterle, A.M.4    Keppeler, H.5    Lauber, K.6
  • 24
    • 84871581862 scopus 로고    scopus 로고
    • Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    • doi:10.1016/j.cell.2012.11.028
    • Ragusa MJ, Stanley RE, Hurley JH. Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell (2012) 151(7):1501-12. doi:10.1016/j.cell.2012.11.028.
    • (2012) Cell , vol.151 , Issue.7 , pp. 1501-1512
    • Ragusa, M.J.1    Stanley, R.E.2    Hurley, J.H.3
  • 25
    • 77950465542 scopus 로고    scopus 로고
    • Current knowledge of the pre-autophagosomal structure (PAS)
    • doi:10.1016/j.febslet.2010.02.001
    • Suzuki K, Ohsumi Y. Current knowledge of the pre-autophagosomal structure (PAS). FEBS Lett (2010) 584(7):1280-6. doi:10.1016/j.febslet.2010.02.001.
    • (2010) FEBS Lett , vol.584 , Issue.7 , pp. 1280-1286
    • Suzuki, K.1    Ohsumi, Y.2
  • 26
    • 79251577061 scopus 로고    scopus 로고
    • The regulation of autophagy-unanswered questions
    • doi:10.1242/jcs.064576
    • Chen Y, Klionsky DJ. The regulation of autophagy-unanswered questions. J Cell Sci (2011) 124(Pt 2):161-70. doi:10.1242/jcs.064576.
    • (2011) J Cell Sci , vol.124 , Issue.PART 2 , pp. 161-170
    • Chen, Y.1    Klionsky, D.J.2
  • 27
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • doi:10.1083/jcb.200803137
    • Axe EL, Walker SA, Manifava M, Chandra P, Roderick HL, Habermann A, et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol (2008) 182(4):685-701. doi:10.1083/jcb.200803137.
    • (2008) J Cell Biol , vol.182 , Issue.4 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6
  • 28
    • 84862626146 scopus 로고    scopus 로고
    • The plasma membrane as a control center for autophagy
    • doi:10.4161/auto.20060
    • Moreau K, Rubinsztein DC. The plasma membrane as a control center for autophagy. Autophagy (2012) 8(5):861-3. doi:10.4161/auto.20060.
    • (2012) Autophagy , vol.8 , Issue.5 , pp. 861-863
    • Moreau, K.1    Rubinsztein, D.C.2
  • 29
    • 75749135725 scopus 로고    scopus 로고
    • The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy
    • doi:10.1083/jcb.200904075
    • Yen WL, Shintani T, Nair U, Cao Y, Richardson BC, Li Z, et al. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. J Cell Biol (2010) 188(1):101-14. doi:10.1083/jcb.200904075.
    • (2010) J Cell Biol , vol.188 , Issue.1 , pp. 101-114
    • Yen, W.L.1    Shintani, T.2    Nair, U.3    Cao, Y.4    Richardson, B.C.5    Li, Z.6
  • 30
    • 77952495224 scopus 로고    scopus 로고
    • Mitochondria supply membranes for autophagosome biogenesis during starvation
    • doi:10.1016/j.cell.2010.04.009
    • Hailey DW, Rambold AS, Satpute-Krishnan P, Mitra K, Sougrat R, Kim PK, et al. Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell (2010) 141(4):656-67. doi:10.1016/j.cell.2010.04.009.
    • (2010) Cell , vol.141 , Issue.4 , pp. 656-667
    • Hailey, D.W.1    Rambold, A.S.2    Satpute-Krishnan, P.3    Mitra, K.4    Sougrat, R.5    Kim, P.K.6
  • 31
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • doi:10.4161/auto.5.8.10274
    • Yla-Anttila P, Vihinen H, Jokitalo E, Eskelinen EL. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy (2009) 5(8):1180-5. doi:10.4161/auto.5.8.10274.
    • (2009) Autophagy , vol.5 , Issue.8 , pp. 1180-1185
    • Yla-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.L.4
  • 32
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • doi:10.1038/ncb1991
    • Hayashi-Nishino M, Fujita N, Noda T, Yamaguchi A, Yoshimori T, Yamamoto A. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol (2009) 11(12):1433-7. doi:10.1038/ncb1991.
    • (2009) Nat Cell Biol , vol.11 , Issue.12 , pp. 1433-1437
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3    Yamaguchi, A.4    Yoshimori, T.5    Yamamoto, A.6
  • 33
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • doi:10.1074/jbc.275.2.992
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem (2000) 275(2):992-8. doi:10.1074/jbc.275.2.992.
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 34
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • doi:10.1093/emboj/19.17.4577
    • Gillooly DJ, Morrow IC, Lindsay M, Gould R, Bryant NJ, Gaullier JM, et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J (2000) 19(17):4577-88. doi:10.1093/emboj/19.17.4577.
    • (2000) EMBO J , vol.19 , Issue.17 , pp. 4577-4588
    • Gillooly, D.J.1    Morrow, I.C.2    Lindsay, M.3    Gould, R.4    Bryant, N.J.5    Gaullier, J.M.6
  • 35
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • doi:10.1038/ncb1854
    • Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol (2009) 11(4):468-76. doi:10.1038/ncb1854.
    • (2009) Nat Cell Biol , vol.11 , Issue.4 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6
  • 36
    • 0028981018 scopus 로고
    • A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system
    • Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, et al. A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J (1995) 14(14):3339-48.
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3339-3348
    • Volinia, S.1    Dhand, R.2    Vanhaesebroeck, B.3    MacDougall, L.K.4    Stein, R.5    Zvelebil, M.J.6
  • 37
    • 77955895424 scopus 로고    scopus 로고
    • Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
    • doi:10.1083/jcb.200911141
    • Matsunaga K, Morita E, Saitoh T, Akira S, Ktistakis NT, Izumi T, et al. Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L. J Cell Biol (2010) 190(4):511-21. doi:10.1083/jcb.200911141.
    • (2010) J Cell Biol , vol.190 , Issue.4 , pp. 511-521
    • Matsunaga, K.1    Morita, E.2    Saitoh, T.3    Akira, S.4    Ktistakis, N.T.5    Izumi, T.6
  • 38
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • doi:10.1038/ncb1846
    • Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, et al. Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol (2009) 11(4):385-96. doi:10.1038/ncb1846.
    • (2009) Nat Cell Biol , vol.11 , Issue.4 , pp. 385-396
    • Matsunaga, K.1    Saitoh, T.2    Tabata, K.3    Omori, H.4    Satoh, T.5    Kurotori, N.6
  • 39
    • 80052145824 scopus 로고    scopus 로고
    • Freeze-fracture replica immunolabelling reveals human WIPI-1 and WIPI-2 as membrane proteins of autophagosomes
    • doi:10.1111/j.1582-4934.2011.01339.x
    • Proikas-Cezanne T, Robenek H. Freeze-fracture replica immunolabelling reveals human WIPI-1 and WIPI-2 as membrane proteins of autophagosomes. J Cell Mol Med (2011) 15(9):2007-10. doi:10.1111/j.1582-4934.2011.01339.x.
    • (2011) J Cell Mol Med , vol.15 , Issue.9 , pp. 2007-2010
    • Proikas-Cezanne, T.1    Robenek, H.2
  • 40
    • 84870893906 scopus 로고    scopus 로고
    • How Atg18 and the WIPIs sense phosphatidylinositol 3-phosphate
    • doi:10.4161/auto.22077
    • Baskaran S, Ragusa MJ, Hurley JH. How Atg18 and the WIPIs sense phosphatidylinositol 3-phosphate. Autophagy (2012) 8(12):1851-2. doi:10.4161/auto.22077.
    • (2012) Autophagy , vol.8 , Issue.12 , pp. 1851-1852
    • Baskaran, S.1    Ragusa, M.J.2    Hurley, J.H.3
  • 41
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • doi:10.4161/auto.6.6.12709
    • Itakura E, Mizushima N. Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy (2010) 6(6):764-76. doi:10.4161/auto.6.6.12709.
    • (2010) Autophagy , vol.6 , Issue.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 42
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • doi:10.4161/auto.6.4.11863
    • Polson HE, de Lartigue J, Rigden DJ, Reedijk M, Urbe S, Clague MJ, et al. Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation. Autophagy (2010) 6(4):506-22. doi:10.4161/auto.6.4.11863.
    • (2010) Autophagy , vol.6 , Issue.4 , pp. 506-522
    • Polson, H.E.1    de Lartigue, J.2    Rigden, D.J.3    Reedijk, M.4    Urbe, S.5    Clague, M.J.6
  • 43
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • doi:10.1016/S1534-5807(03)00402-7
    • Reggiori F, Tucker KA, Stromhaug PE, Klionsky DJ. The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure. Dev Cell (2004) 6(1):79-90. doi:10.1016/S1534-5807(03)00402-7.
    • (2004) Dev Cell , vol.6 , Issue.1 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 44
    • 84857844643 scopus 로고    scopus 로고
    • Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets
    • doi:10.1091/mbc. E11-09-0785
    • Velikkakath AK, Nishimura T, Oita E, Ishihara N, Mizushima N. Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets. Mol Biol Cell (2012) 23(5):896-909. doi:10.1091/mbc. E11-09-0785.
    • (2012) Mol Biol Cell , vol.23 , Issue.5 , pp. 896-909
    • Velikkakath, A.K.1    Nishimura, T.2    Oita, E.3    Ishihara, N.4    Mizushima, N.5
  • 45
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • doi:10.1083/jcb.200912089
    • Mari M, Griffith J, Rieter E, Krishnappa L, Klionsky DJ, Reggiori F. An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J Cell Biol (2010) 190(6):1005-22. doi:10.1083/jcb.200912089.
    • (2010) J Cell Biol , vol.190 , Issue.6 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krishnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 46
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy
    • doi:10.1091/mbc. E11-09-0746
    • Orsi A, Razi M, Dooley HC, Robinson D, Weston AE, Collinson LM, et al. Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol Biol Cell (2012) 23(10):1860-73. doi:10.1091/mbc. E11-09-0746.
    • (2012) Mol Biol Cell , vol.23 , Issue.10 , pp. 1860-1873
    • Orsi, A.1    Razi, M.2    Dooley, H.C.3    Robinson, D.4    Weston, A.E.5    Collinson, L.M.6
  • 47
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • doi:10.1242/jcs.03172
    • Young AR, Chan EY, Hu XW, Kochl R, Crawshaw SG, High S, et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci (2006) 119(Pt 18):3888-900. doi:10.1242/jcs.03172.
    • (2006) J Cell Sci , vol.119 , Issue.PART 18 , pp. 3888-3900
    • Young, A.R.1    Chan, E.Y.2    Hu, X.W.3    Kochl, R.4    Crawshaw, S.G.5    High, S.6
  • 48
    • 84864991509 scopus 로고    scopus 로고
    • Atg9 vesicles are an important membrane source during early steps of autophagosome formation
    • doi:10.1083/jcb.201202061
    • Yamamoto H, Kakuta S, Watanabe TM, Kitamura A, Sekito T, Kondo-Kakuta C, et al. Atg9 vesicles are an important membrane source during early steps of autophagosome formation. J Cell Biol (2012) 198(2):219-33. doi:10.1083/jcb.201202061.
    • (2012) J Cell Biol , vol.198 , Issue.2 , pp. 219-233
    • Yamamoto, H.1    Kakuta, S.2    Watanabe, T.M.3    Kitamura, A.4    Sekito, T.5    Kondo-Kakuta, C.6
  • 49
    • 79959874238 scopus 로고    scopus 로고
    • The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella
    • doi:10.1091/mbc. E10-11-0893
    • Kageyama S, Omori H, Saitoh T, Sone T, Guan JL, Akira S, et al. The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella. Mol Biol Cell (2011) 22(13):2290-300. doi:10.1091/mbc. E10-11-0893.
    • (2011) Mol Biol Cell , vol.22 , Issue.13 , pp. 2290-2300
    • Kageyama, S.1    Omori, H.2    Saitoh, T.3    Sone, T.4    Guan, J.L.5    Akira, S.6
  • 50
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • doi:10.4161/auto.19496
    • Klionsky DJ, Abdalla FC, Abeliovich H, Abraham RT, Acevedo-Arozena A, Adeli K, et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy (2012) 8(4):445-544. doi:10.4161/auto.19496.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
    • Klionsky, D.J.1    Abdalla, F.C.2    Abeliovich, H.3    Abraham, R.T.4    Acevedo-Arozena, A.5    Adeli, K.6
  • 51
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy
    • doi:10.1074/jbc.273.51.33889
    • Mizushima N, Sugita H, Yoshimori T, Ohsumi Y. A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy. J Biol Chem (1998) 273(51):33889-92. doi:10.1074/jbc.273.51.33889.
    • (1998) J Biol Chem , vol.273 , Issue.51 , pp. 33889-92
    • Mizushima, N.1    Sugita, H.2    Yoshimori, T.3    Ohsumi, Y.4
  • 52
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • doi:10.1242/jcs.00381
    • Mizushima N, Kuma A, Kobayashi Y, Yamamoto A, Matsubae M, Takao T, et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J Cell Sci (2003) 116(Pt 9):1679-88. doi:10.1242/jcs.00381.
    • (2003) J Cell Sci , vol.116 , Issue.PART 9 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3    Yamamoto, A.4    Matsubae, M.5    Takao, T.6
  • 53
    • 0347695019 scopus 로고    scopus 로고
    • A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • doi:10.1074/jbc. M308762200
    • Hemelaar J, Lelyveld VS, Kessler BM, Ploegh HL. A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J Biol Chem (2003) 278(51):51841-50. doi:10.1074/jbc. M308762200.
    • (2003) J Biol Chem , vol.278 , Issue.51 , pp. 51841-50
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 54
    • 80555144189 scopus 로고    scopus 로고
    • Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway
    • doi:10.1016/j.molcel.2011.08.034
    • Taherbhoy AM, Tait SW, Kaiser SE, Williams AH, Deng A, Nourse A, et al. Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol Cell (2011) 44(3):451-61. doi:10.1016/j.molcel.2011.08.034.
    • (2011) Mol Cell , vol.44 , Issue.3 , pp. 451-461
    • Taherbhoy, A.M.1    Tait, S.W.2    Kaiser, S.E.3    Williams, A.H.4    Deng, A.5    Nourse, A.6
  • 55
    • 0141960205 scopus 로고    scopus 로고
    • The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification
    • doi:10.1074/jbc. M300550200
    • Nemoto T, Tanida I, Tanida-Miyake E, Minematsu-Ikeguchi N, Yokota M, Ohsumi M, et al. The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification. J Biol Chem (2003) 278(41):39517-26. doi:10.1074/jbc. M300550200.
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 39517-26
    • Nemoto, T.1    Tanida, I.2    Tanida-Miyake, E.3    Minematsu-Ikeguchi, N.4    Yokota, M.5    Ohsumi, M.6
  • 56
    • 57549094368 scopus 로고    scopus 로고
    • The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice
    • doi:10.1091/mbc. E08-03-0309
    • Sou YS, Waguri S, Iwata J, Ueno T, Fujimura T, Hara T, et al. The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice. Mol Biol Cell (2008) 19(11):4762-75. doi:10.1091/mbc. E08-03-0309.
    • (2008) Mol Biol Cell , vol.19 , Issue.11 , pp. 4762-4775
    • Sou, Y.S.1    Waguri, S.2    Iwata, J.3    Ueno, T.4    Fujimura, T.5    Hara, T.6
  • 57
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • doi:10.1074/jbc. C700195200
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, Takao T, et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem (2007) 282(52):37298-302. doi:10.1074/jbc. C700195200.
    • (2007) J Biol Chem , vol.282 , Issue.52 , pp. 37298-302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6
  • 58
    • 84866158316 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-phosphate clearance plays a key role in autophagosome completion
    • doi:10.1016/j.cub.2012.06.029
    • Cebollero E, van der Vaart A, Zhao M, Rieter E, Klionsky DJ, Helms JB, et al. Phosphatidylinositol-3-phosphate clearance plays a key role in autophagosome completion. Curr Biol (2012) 22(17):1545-53. doi:10.1016/j.cub.2012.06.029.
    • (2012) Curr Biol , vol.22 , Issue.17 , pp. 1545-1553
    • Cebollero, E.1    van der Vaart, A.2    Zhao, M.3    Rieter, E.4    Klionsky, D.J.5    Helms, J.B.6
  • 59
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • doi:10.1083/jcb.200702115
    • Filimonenko M, Stuffers S, Raiborg C, Yamamoto A, Malerod L, Fisher EM, et al. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol (2007) 179(3):485-500. doi:10.1083/jcb.200702115.
    • (2007) J Cell Biol , vol.179 , Issue.3 , pp. 485-500
    • Filimonenko, M.1    Stuffers, S.2    Raiborg, C.3    Yamamoto, A.4    Malerod, L.5    Fisher, E.M.6
  • 60
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • doi:10.1016/j.cell.2012.11.001
    • Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell (2012) 151(6):1256-69. doi:10.1016/j.cell.2012.11.001.
    • (2012) Cell , vol.151 , Issue.6 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 61
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • doi:10.1242/jcs.01114
    • Gutierrez MG, Munafo DB, Beron W, Colombo MI. Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J Cell Sci (2004) 117(Pt 13):2687-97. doi:10.1242/jcs.01114.
    • (2004) J Cell Sci , vol.117 , Issue.PART 13 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafo, D.B.2    Beron, W.3    Colombo, M.I.4
  • 62
    • 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
    • Liang C, Lee JS, Inn KS, Gack MU, Li Q, Roberts EA, et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat Cell Biol (2008) 10(7):776-87. doi:10.1038/ncb1740.
    • (2008) Nat Cell Biol , 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
  • 63
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • doi:10.1083/jcb.200907015
    • Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, Overvatn A, et al. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol (2010) 188(2):253-69. doi:10.1083/jcb.200907015.
    • (2010) J Cell Biol , vol.188 , Issue.2 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5    Overvatn, A.6
  • 64
    • 28244493702 scopus 로고    scopus 로고
    • Participation of autophagy in storage of lysosomes in neurons from mouse models of neuronal ceroid-lipofuscinoses (Batten disease)
    • doi:10.1016/S0002-9440(10)61253-9
    • Koike M, Shibata M, Waguri S, Yoshimura K, Tanida I, Kominami E, et al. Participation of autophagy in storage of lysosomes in neurons from mouse models of neuronal ceroid-lipofuscinoses (Batten disease). Am J Pathol (2005) 167(6):1713-28. doi:10.1016/S0002-9440(10)61253-9.
    • (2005) Am J Pathol , vol.167 , Issue.6 , pp. 1713-1728
    • Koike, M.1    Shibata, M.2    Waguri, S.3    Yoshimura, K.4    Tanida, I.5    Kominami, E.6
  • 65
    • 84869034809 scopus 로고    scopus 로고
    • Reduced cathepsins B and D cause impaired autophagic degradation that can be almost completely restored by overexpression of these two proteases in Sap C-deficient fibroblasts
    • doi:10.1093/hmg/dds367
    • Tatti M, Motta M, Di Bartolomeo S, Scarpa S, Cianfanelli V, Cecconi F, et al. Reduced cathepsins B and D cause impaired autophagic degradation that can be almost completely restored by overexpression of these two proteases in Sap C-deficient fibroblasts. Hum Mol Genet (2012) 21(23):5159-73. doi:10.1093/hmg/dds367.
    • (2012) Hum Mol Genet , vol.21 , Issue.23 , pp. 5159-5173
    • Tatti, M.1    Motta, M.2    Di Bartolomeo, S.3    Scarpa, S.4    Cianfanelli, V.5    Cecconi, F.6
  • 66
    • 79956346329 scopus 로고    scopus 로고
    • Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation
    • doi:10.1073/pnas.1013800108
    • Rong Y, McPhee CK, Deng S, Huang L, Chen L, Liu M, et al. Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation. Proc Natl Acad Sci U S A (2011) 108(19):7826-31. doi:10.1073/pnas.1013800108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.19 , pp. 7826-7831
    • Rong, Y.1    McPhee, C.K.2    Deng, S.3    Huang, L.4    Chen, L.5    Liu, M.6
  • 67
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • doi:10.1038/nature09076
    • Yu L, McPhee CK, Zheng L, Mardones GA, Rong Y, Peng J, et al. Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature (2010) 465(7300):942-6. doi:10.1038/nature09076.
    • (2010) Nature , vol.465 , Issue.7300 , pp. 942-946
    • Yu, L.1    McPhee, C.K.2    Zheng, L.3    Mardones, G.A.4    Rong, Y.5    Peng, J.6
  • 68
    • 84969213492 scopus 로고    scopus 로고
    • Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls
    • Wellcome Trust Case Control Consortium. doi:10.1038/nature05911
    • Wellcome Trust Case Control Consortium. Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls. Nature (2007) 447(7145):661-78. doi:10.1038/nature05911.
    • (2007) Nature , vol.447 , Issue.7145 , pp. 661-678
  • 69
    • 33846627302 scopus 로고    scopus 로고
    • A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1
    • doi:10.1038/ng1954
    • Hampe J, Franke A, Rosenstiel P, Till A, Teuber M, Huse K, et al. A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1. Nat Genet (2007) 39(2):207-11. doi:10.1038/ng1954.
    • (2007) Nat Genet , vol.39 , Issue.2 , pp. 207-211
    • Hampe, J.1    Franke, A.2    Rosenstiel, P.3    Till, A.4    Teuber, M.5    Huse, K.6
  • 70
    • 48349136889 scopus 로고    scopus 로고
    • Genome-wide association defines more than 30 distinct susceptibility loci for Crohn's disease
    • doi:10.1038/ng.175
    • Barrett JC, Hansoul S, Nicolae DL, Cho JH, Duerr RH, Rioux JD, et al. Genome-wide association defines more than 30 distinct susceptibility loci for Crohn's disease. Nat Genet (2008) 40(8):955-62. doi:10.1038/ng.175.
    • (2008) Nat Genet , vol.40 , Issue.8 , pp. 955-962
    • Barrett, J.C.1    Hansoul, S.2    Nicolae, D.L.3    Cho, J.H.4    Duerr, R.H.5    Rioux, J.D.6
  • 71
    • 78649489009 scopus 로고    scopus 로고
    • Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci
    • doi:10.1038/ng.717
    • Franke A, McGovern DP, Barrett JC, Wang K, Radford-Smith GL, Ahmad T, et al. Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci. Nat Genet (2010) 42(12):1118-25. doi:10.1038/ng.717.
    • (2010) Nat Genet , vol.42 , Issue.12 , pp. 1118-1125
    • Franke, A.1    McGovern, D.P.2    Barrett, J.C.3    Wang, K.4    Radford-Smith, G.L.5    Ahmad, T.6
  • 72
    • 84858642947 scopus 로고    scopus 로고
    • PTPN2 gene variants are associated with susceptibility to both Crohn's disease and ulcerative colitis supporting a common genetic disease background
    • doi:10.1371/journal.pone.0033682
    • Glas J, Wagner J, Seiderer J, Olszak T, Wetzke M, Beigel F, et al. PTPN2 gene variants are associated with susceptibility to both Crohn's disease and ulcerative colitis supporting a common genetic disease background. PLoS ONE (2012) 7(3):e33682. doi:10.1371/journal.pone.0033682.
    • (2012) PLoS ONE , vol.7 , Issue.3
    • Glas, J.1    Wagner, J.2    Seiderer, J.3    Olszak, T.4    Wetzke, M.5    Beigel, F.6
  • 73
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • doi:10.1038/ng2032
    • Rioux JD, Xavier RJ, Taylor KD, Silverberg MS, Goyette P, Huett A, et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat Genet (2007) 39(5):596-604. doi:10.1038/ng2032.
    • (2007) Nat Genet , vol.39 , Issue.5 , pp. 596-604
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3    Silverberg, M.S.4    Goyette, P.5    Huett, A.6
  • 74
    • 0033565655 scopus 로고    scopus 로고
    • Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
    • doi:10.1093/emboj/18.14.3888
    • Mizushima N, Noda T, Ohsumi Y. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J (1999) 18(14):3888-96. doi:10.1093/emboj/18.14.3888.
    • (1999) EMBO J , vol.18 , Issue.14 , pp. 3888-3896
    • Mizushima, N.1    Noda, T.2    Ohsumi, Y.3
  • 75
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • doi:10.1038/nature07383
    • Saitoh T, Fujita N, Jang MH, Uematsu S, Yang BG, Satoh T, et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature (2008) 456(7219):264-8. doi:10.1038/nature07383.
    • (2008) Nature , vol.456 , Issue.7219 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3    Uematsu, S.4    Yang, B.G.5    Satoh, T.6
  • 76
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • doi:10.1038/nature07416
    • Cadwell K, Liu JY, Brown SL, Miyoshi H, Loh J, Lennerz JK, et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature (2008) 456(7219):259-63. doi:10.1038/nature07416.
    • (2008) Nature , vol.456 , Issue.7219 , pp. 259-263
    • Cadwell, K.1    Liu, J.Y.2    Brown, S.L.3    Miyoshi, H.4    Loh, J.5    Lennerz, J.K.6
  • 77
    • 84860136921 scopus 로고    scopus 로고
    • Abnormal activation of autophagy-induced crinophagy in Paneth cells from patients with Crohn's disease
    • doi:10.1053/j.gastro.2012.01.031
    • Thachil E, Hugot JP, Arbeille B, Paris R, Grodet A, Peuchmaur M, et al. Abnormal activation of autophagy-induced crinophagy in Paneth cells from patients with Crohn's disease. Gastroenterology (2012) 142(5):1097e-9e. doi:10.1053/j.gastro.2012.01.031.
    • (2012) Gastroenterology , vol.142 , Issue.5
    • Thachil, E.1    Hugot, J.P.2    Arbeille, B.3    Paris, R.4    Grodet, A.5    Peuchmaur, M.6
  • 78
    • 80051550866 scopus 로고    scopus 로고
    • Crohn's disease-associated ATG16L1 polymorphism modulates pro-inflammatory cytokine responses selectively upon activation of NOD2
    • doi:10.1136/gut.2010.228908
    • Plantinga TS, Crisan TO, Oosting M, van de Veerdonk FL, de Jong DJ, Philpott DJ, et al. Crohn's disease-associated ATG16L1 polymorphism modulates pro-inflammatory cytokine responses selectively upon activation of NOD2. Gut (2011) 60(9):1229-35. doi:10.1136/gut.2010.228908.
    • (2011) Gut , vol.60 , Issue.9 , pp. 1229-1235
    • Plantinga, T.S.1    Crisan, T.O.2    Oosting, M.3    van de Veerdonk, F.L.4    de Jong, D.J.5    Philpott, D.J.6
  • 79
    • 84863078686 scopus 로고    scopus 로고
    • Autophagy suppresses interleukin-1beta (IL-1beta) signaling by activation of p62 degradation via lysosomal and proteasomal pathways
    • doi:10.1074/jbc. M111.280065
    • Lee J, Kim HR, Quinley C, Kim J, Gonzalez-Navajas J, Xavier R, et al. Autophagy suppresses interleukin-1beta (IL-1beta) signaling by activation of p62 degradation via lysosomal and proteasomal pathways. J Biol Chem (2012) 287(6):4033-40. doi:10.1074/jbc. M111.280065.
    • (2012) J Biol Chem , vol.287 , Issue.6 , pp. 4033-4040
    • Lee, J.1    Kim, H.R.2    Quinley, C.3    Kim, J.4    Gonzalez-Navajas, J.5    Xavier, R.6
  • 80
    • 84886779930 scopus 로고    scopus 로고
    • Three isoforms of the Atg16L1 protein contribute different autophagic properties
    • doi:10.1007/s11010-013-1616-8
    • Jiang T, Qin B, He J, Lin S, Ding S. Three isoforms of the Atg16L1 protein contribute different autophagic properties. Mol Cell Biochem (2013) 378(1-2):257-66. doi:10.1007/s11010-013-1616-8.
    • (2013) Mol Cell Biochem , vol.378 , Issue.1-2 , pp. 257-266
    • Jiang, T.1    Qin, B.2    He, J.3    Lin, S.4    Ding, S.5
  • 81
    • 0036218221 scopus 로고    scopus 로고
    • The immunology of mucosal models of inflammation
    • doi:10.1146/annurev.immunol.20.100301.064816
    • Strober W, Fuss IJ, Blumberg RS. The immunology of mucosal models of inflammation. Annu Rev Immunol (2002) 20:495-549. doi:10.1146/annurev.immunol.20.100301.064816.
    • (2002) Annu Rev Immunol , vol.20 , pp. 495-549
    • Strober, W.1    Fuss, I.J.2    Blumberg, R.S.3
  • 82
    • 77953904042 scopus 로고    scopus 로고
    • Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine
    • doi:10.1016/j.cell.2010.05.009
    • Cadwell K, Patel KK, Maloney NS, Liu TC, Ng AC, Storer CE, et al. Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine. Cell (2010) 141(7):1135-45. doi:10.1016/j.cell.2010.05.009.
    • (2010) Cell , vol.141 , Issue.7 , pp. 1135-1145
    • Cadwell, K.1    Patel, K.K.2    Maloney, N.S.3    Liu, T.C.4    Ng, A.C.5    Storer, C.E.6
  • 83
    • 80051483002 scopus 로고    scopus 로고
    • Distinct and overlapping genetic loci in Crohn's disease and ulcerative colitis: correlations with pathogenesis
    • doi:10.1002/ibd.21579
    • Waterman M, Xu W, Stempak JM, Milgrom R, Bernstein CN, Griffiths AM, et al. Distinct and overlapping genetic loci in Crohn's disease and ulcerative colitis: correlations with pathogenesis. Inflamm Bowel Dis (2011) 17(9):1936-42. doi:10.1002/ibd.21579.
    • (2011) Inflamm Bowel Dis , vol.17 , Issue.9 , pp. 1936-1942
    • Waterman, M.1    Xu, W.2    Stempak, J.M.3    Milgrom, R.4    Bernstein, C.N.5    Griffiths, A.M.6
  • 84
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • doi:10.1038/35079114
    • Ogura Y, Bonen DK, Inohara N, Nicolae DL, Chen FF, Ramos R, et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature (2001) 411(6837):603-6. doi:10.1038/35079114.
    • (2001) Nature , vol.411 , Issue.6837 , pp. 603-606
    • Ogura, Y.1    Bonen, D.K.2    Inohara, N.3    Nicolae, D.L.4    Chen, F.F.5    Ramos, R.6
  • 85
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • doi:10.1074/jbc. C200651200
    • Girardin SE, Boneca IG, Viala J, Chamaillard M, Labigne A, Thomas G, et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem (2003) 278(11):8869-72. doi:10.1074/jbc. C200651200.
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 8869-8872
    • Girardin, S.E.1    Boneca, I.G.2    Viala, J.3    Chamaillard, M.4    Labigne, A.5    Thomas, G.6
  • 86
    • 73849121209 scopus 로고    scopus 로고
    • Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry
    • doi:10.1038/ni.1823
    • Travassos LH, Carneiro LA, Ramjeet M, Hussey S, Kim YG, Magalhaes JG, et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat Immunol (2010) 11(1):55-62. doi:10.1038/ni.1823.
    • (2010) Nat Immunol , vol.11 , Issue.1 , pp. 55-62
    • Travassos, L.H.1    Carneiro, L.A.2    Ramjeet, M.3    Hussey, S.4    Kim, Y.G.5    Magalhaes, J.G.6
  • 87
    • 73849151394 scopus 로고    scopus 로고
    • NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation
    • doi:10.1038/nm.2069
    • Cooney R, Baker J, Brain O, Danis B, Pichulik T, Allan P, et al. NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation. Nat Med (2010) 16(1):90-7. doi:10.1038/nm.2069.
    • (2010) Nat Med , vol.16 , Issue.1 , pp. 90-97
    • Cooney, R.1    Baker, J.2    Brain, O.3    Danis, B.4    Pichulik, T.5    Allan, P.6
  • 88
    • 84874253948 scopus 로고    scopus 로고
    • IRGM in autophagy and viral infections
    • doi:10.3389/fimmu.2012.00426
    • Petkova DS, Viret C, Faure M. IRGM in autophagy and viral infections. Front Immunol (2012) 3:426. doi:10.3389/fimmu.2012.00426.
    • (2012) Front Immunol , vol.3 , pp. 426
    • Petkova, D.S.1    Viret, C.2    Faure, M.3
  • 89
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • doi:10.1126/science.1129577
    • Singh SB, Davis AS, Taylor GA, Deretic V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science (2006) 313(5792):1438-41. doi:10.1126/science.1129577.
    • (2006) Science , vol.313 , Issue.5792 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 90
    • 84861186087 scopus 로고    scopus 로고
    • Defects in autophagy favour adherent-invasive Escherichia coli persistence within macrophages leading to increased pro-inflammatory response
    • doi:10.1111/j.1462-5822.2012.01768.x
    • Lapaquette P, Bringer MA, Darfeuille-Michaud A. Defects in autophagy favour adherent-invasive Escherichia coli persistence within macrophages leading to increased pro-inflammatory response. Cell Microbiol (2012) 14(6):791-807. doi:10.1111/j.1462-5822.2012.01768.x.
    • (2012) Cell Microbiol , vol.14 , Issue.6 , pp. 791-807
    • Lapaquette, P.1    Bringer, M.A.2    Darfeuille-Michaud, A.3
  • 91
    • 34347338690 scopus 로고    scopus 로고
    • Sequence variants in the autophagy gene IRGM and multiple other replicating loci contribute to Crohn's disease susceptibility
    • doi:10.1038/ng2061
    • Parkes M, Barrett JC, Prescott NJ, Tremelling M, Anderson CA, Fisher SA, et al. Sequence variants in the autophagy gene IRGM and multiple other replicating loci contribute to Crohn's disease susceptibility. Nat Genet (2007) 39(7):830-2. doi:10.1038/ng2061.
    • (2007) Nat Genet , vol.39 , Issue.7 , pp. 830-832
    • Parkes, M.1    Barrett, J.C.2    Prescott, N.J.3    Tremelling, M.4    Anderson, C.A.5    Fisher, S.A.6
  • 92
    • 50449091647 scopus 로고    scopus 로고
    • Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease
    • doi:10.1038/ng.215
    • McCarroll SA, Huett A, Kuballa P, Chilewski SD, Landry A, Goyette P, et al. Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease. Nat Genet (2008) 40(9):1107-12. doi:10.1038/ng.215.
    • (2008) Nat Genet , vol.40 , Issue.9 , pp. 1107-1112
    • McCarroll, S.A.1    Huett, A.2    Kuballa, P.3    Chilewski, S.D.4    Landry, A.5    Goyette, P.6
  • 93
    • 79952134938 scopus 로고    scopus 로고
    • A synonymous variant in IRGM alters a binding site for miR-196 and causes deregulation of IRGM-dependent xenophagy in Crohn's disease
    • doi:10.1038/ng.762
    • Brest P, Lapaquette P, Souidi M, Lebrigand K, Cesaro A, Vouret-Craviari V, et al. A synonymous variant in IRGM alters a binding site for miR-196 and causes deregulation of IRGM-dependent xenophagy in Crohn's disease. Nat Genet (2011) 43(3):242-5. doi:10.1038/ng.762.
    • (2011) Nat Genet , vol.43 , Issue.3 , pp. 242-245
    • Brest, P.1    Lapaquette, P.2    Souidi, M.3    Lebrigand, K.4    Cesaro, A.5    Vouret-Craviari, V.6
  • 94
    • 4143069158 scopus 로고    scopus 로고
    • High prevalence of adherent-invasive Escherichia coli associated with ileal mucosa in Crohn's disease
    • doi:10.1053/j.gastro.2004.04.061
    • Darfeuille-Michaud A, Boudeau J, Bulois P, Neut C, Glasser AL, Barnich N, et al. High prevalence of adherent-invasive Escherichia coli associated with ileal mucosa in Crohn's disease. Gastroenterology (2004) 127(2):412-21. doi:10.1053/j.gastro.2004.04.061.
    • (2004) Gastroenterology , vol.127 , Issue.2 , pp. 412-421
    • Darfeuille-Michaud, A.1    Boudeau, J.2    Bulois, P.3    Neut, C.4    Glasser, A.L.5    Barnich, N.6
  • 95
    • 67649509224 scopus 로고    scopus 로고
    • Molecular diversity of Escherichia coli in the human gut: new ecological evidence supporting the role of adherent-invasive E. coli (AIEC) in Crohn's disease
    • doi:10.1002/ibd.20860
    • Martinez-Medina M, Aldeguer X, Lopez-Siles M, Gonzalez-Huix F, Lopez-Oliu C, Dahbi G, et al. Molecular diversity of Escherichia coli in the human gut: new ecological evidence supporting the role of adherent-invasive E. coli (AIEC) in Crohn's disease. Inflamm Bowel Dis (2009) 15(6):872-82. doi:10.1002/ibd.20860.
    • (2009) Inflamm Bowel Dis , vol.15 , Issue.6 , pp. 872-882
    • Martinez-Medina, M.1    Aldeguer, X.2    Lopez-Siles, M.3    Gonzalez-Huix, F.4    Lopez-Oliu, C.5    Dahbi, G.6
  • 96
    • 44349136821 scopus 로고    scopus 로고
    • Genetic determinants of ulcerative colitis include the ECM1 locus and five loci implicated in Crohn's disease
    • doi:10.1038/ng.145
    • Fisher SA, Tremelling M, Anderson CA, Gwilliam R, Bumpstead S, Prescott NJ, et al. Genetic determinants of ulcerative colitis include the ECM1 locus and five loci implicated in Crohn's disease. Nat Genet (2008) 40(6):710-2. doi:10.1038/ng.145.
    • (2008) Nat Genet , vol.40 , Issue.6 , pp. 710-712
    • Fisher, S.A.1    Tremelling, M.2    Anderson, C.A.3    Gwilliam, R.4    Bumpstead, S.5    Prescott, N.J.6
  • 97
    • 77951782697 scopus 로고    scopus 로고
    • Susceptibility loci reported in genome-wide association studies are associated with Crohn's disease in Canadian children
    • doi:10.1111/j.1365-2036.2010.04294.x
    • Amre DK, Mack DR, Morgan K, Israel D, Deslandres C, Seidman EG, et al. Susceptibility loci reported in genome-wide association studies are associated with Crohn's disease in Canadian children. Aliment Pharmacol Ther (2010) 31(11):1186-91. doi:10.1111/j.1365-2036.2010.04294.x.
    • (2010) Aliment Pharmacol Ther , vol.31 , Issue.11 , pp. 1186-1191
    • Amre, D.K.1    Mack, D.R.2    Morgan, K.3    Israel, D.4    Deslandres, C.5    Seidman, E.G.6
  • 98
    • 84858683881 scopus 로고    scopus 로고
    • Crohn's disease-associated polymorphism within the PTPN2 gene affects muramyl-dipeptide-induced cytokine secretion and autophagy
    • doi:10.1002/ibd.21913
    • Scharl M, Mwinyi J, Fischbeck A, Leucht K, Eloranta JJ, Arikkat J, et al. Crohn's disease-associated polymorphism within the PTPN2 gene affects muramyl-dipeptide-induced cytokine secretion and autophagy. Inflamm Bowel Dis (2012) 18(5):900-12. doi:10.1002/ibd.21913.
    • (2012) Inflamm Bowel Dis , vol.18 , Issue.5 , pp. 900-912
    • Scharl, M.1    Mwinyi, J.2    Fischbeck, A.3    Leucht, K.4    Eloranta, J.J.5    Arikkat, J.6
  • 99
    • 84861975912 scopus 로고    scopus 로고
    • Regulation of epithelial barrier function by the inflammatory bowel disease candidate gene, PTPN2
    • doi:10.1111/j.1749-6632.2012.06522.x
    • McCole DF. Regulation of epithelial barrier function by the inflammatory bowel disease candidate gene, PTPN2. Ann N Y Acad Sci (2012) 1257:108-14. doi:10.1111/j.1749-6632.2012.06522.x.
    • (2012) Ann N Y Acad Sci , vol.1257 , pp. 108-114
    • McCole, D.F.1
  • 100
    • 1942489307 scopus 로고    scopus 로고
    • T-cell protein tyrosine phosphatase deletion results in progressive systemic inflammatory disease
    • doi:10.1182/blood-2003-09-3153
    • Heinonen KM, Nestel FP, Newell EW, Charette G, Seemayer TA, Tremblay ML, et al. T-cell protein tyrosine phosphatase deletion results in progressive systemic inflammatory disease. Blood (2004) 103(9):3457-64. doi:10.1182/blood-2003-09-3153.
    • (2004) Blood , vol.103 , Issue.9 , pp. 3457-3464
    • Heinonen, K.M.1    Nestel, F.P.2    Newell, E.W.3    Charette, G.4    Seemayer, T.A.5    Tremblay, M.L.6
  • 101
    • 0030769147 scopus 로고    scopus 로고
    • Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice
    • doi:10.1084/jem.186.5.683
    • You-Ten KE, Muise ES, Itie A, Michaliszyn E, Wagner J, Jothy S, et al. Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice. J Exp Med (1997) 186(5):683-93. doi:10.1084/jem.186.5.683.
    • (1997) J Exp Med , vol.186 , Issue.5 , pp. 683-693
    • You-Ten, K.E.1    Muise, E.S.2    Itie, A.3    Michaliszyn, E.4    Wagner, J.5    Jothy, S.6
  • 102
    • 84055191068 scopus 로고    scopus 로고
    • T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice
    • doi:10.1172/JCI59492
    • Wiede F, Shields BJ, Chew SH, Kyparissoudis K, van Vliet C, Galic S, et al. T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice. J Clin Invest (2011) 121(12):4758-74. doi:10.1172/JCI59492.
    • (2011) J Clin Invest , vol.121 , Issue.12 , pp. 4758-4774
    • Wiede, F.1    Shields, B.J.2    Chew, S.H.3    Kyparissoudis, K.4    van Vliet, C.5    Galic, S.6
  • 103
    • 77749258191 scopus 로고    scopus 로고
    • Increased susceptibility to dextran sulfate sodium induced colitis in the T cell protein tyrosine phosphatase heterozygous mouse
    • doi:10.1371/journal.pone.0008868
    • Hassan SW, Doody KM, Hardy S, Uetani N, Cournoyer D, Tremblay ML. Increased susceptibility to dextran sulfate sodium induced colitis in the T cell protein tyrosine phosphatase heterozygous mouse. PLoS ONE (2010) 5(1):e8868. doi:10.1371/journal.pone.0008868.
    • (2010) PLoS ONE , vol.5 , Issue.1
    • Hassan, S.W.1    Doody, K.M.2    Hardy, S.3    Uetani, N.4    Cournoyer, D.5    Tremblay, M.L.6
  • 104
    • 78651070199 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase N2 regulates TNFalpha-induced signalling and cytokine secretion in human intestinal epithelial cells
    • doi:10.1136/gut.2010.216606
    • Scharl M, McCole DF, Weber A, Vavricka SR, Frei P, Kellermeier S, et al. Protein tyrosine phosphatase N2 regulates TNFalpha-induced signalling and cytokine secretion in human intestinal epithelial cells. Gut (2011) 60(2):189-97. doi:10.1136/gut.2010.216606.
    • (2011) Gut , vol.60 , Issue.2 , pp. 189-197
    • Scharl, M.1    McCole, D.F.2    Weber, A.3    Vavricka, S.R.4    Frei, P.5    Kellermeier, S.6
  • 105
    • 70649104669 scopus 로고    scopus 로고
    • Protection of epithelial barrier function by the Crohn's disease associated gene protein tyrosine phosphatase n2
    • doi:10.1053/j.gastro.2009.07.078
    • Scharl M, Paul G, Weber A, Jung BC, Docherty MJ, Hausmann M, et al. Protection of epithelial barrier function by the Crohn's disease associated gene protein tyrosine phosphatase n2. Gastroenterology (2009) 137(6):2030e-40e. doi:10.1053/j.gastro.2009.07.078.
    • (2009) Gastroenterology , vol.137 , Issue.6
    • Scharl, M.1    Paul, G.2    Weber, A.3    Jung, B.C.4    Docherty, M.J.5    Hausmann, M.6
  • 106
    • 84862194557 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase nonreceptor type 2 regulates autophagosome formation in human intestinal cells
    • doi:10.1002/ibd.21891
    • Scharl M, Wojtal KA, Becker HM, Fischbeck A, Frei P, Arikkat J, et al. Protein tyrosine phosphatase nonreceptor type 2 regulates autophagosome formation in human intestinal cells. Inflamm Bowel Dis (2012) 18(7):1287-302. doi:10.1002/ibd.21891.
    • (2012) Inflamm Bowel Dis , vol.18 , Issue.7 , pp. 1287-1302
    • Scharl, M.1    Wojtal, K.A.2    Becker, H.M.3    Fischbeck, A.4    Frei, P.5    Arikkat, J.6
  • 107
    • 84861994381 scopus 로고    scopus 로고
    • The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation
    • doi:10.1111/j.1749-6632.2012.06578.x
    • Scharl M, Rogler G. The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation. Ann N Y Acad Sci (2012) 1257:93-102. doi:10.1111/j.1749-6632.2012.06578.x.
    • (2012) Ann N Y Acad Sci , vol.1257 , pp. 93-102
    • Scharl, M.1    Rogler, G.2
  • 108
    • 84866346322 scopus 로고    scopus 로고
    • Intestinal epithelial cells with impaired autophagy lose their adhesive capacity in the presence of TNF-alpha
    • doi:10.1007/s10620-012-2133-4
    • Saito M, Katsuno T, Nakagawa T, Sato T, Noguchi Y, Sazuka S, et al. Intestinal epithelial cells with impaired autophagy lose their adhesive capacity in the presence of TNF-alpha. Dig Dis Sci (2012) 57(8):2022-30. doi:10.1007/s10620-012-2133-4.
    • (2012) Dig Dis Sci , vol.57 , Issue.8 , pp. 2022-2030
    • Saito, M.1    Katsuno, T.2    Nakagawa, T.3    Sato, T.4    Noguchi, Y.5    Sazuka, S.6
  • 109
    • 50249086073 scopus 로고    scopus 로고
    • XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease
    • doi:10.1016/j.cell.2008.07.021
    • Kaser A, Lee AH, Franke A, Glickman JN, Zeissig S, Tilg H, et al. XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell (2008) 134(5):743-56. doi:10.1016/j.cell.2008.07.021.
    • (2008) Cell , vol.134 , Issue.5 , pp. 743-756
    • Kaser, A.1    Lee, A.H.2    Franke, A.3    Glickman, J.N.4    Zeissig, S.5    Tilg, H.6
  • 110
    • 79955790354 scopus 로고    scopus 로고
    • Genetic variation in the autophagy gene ULK1 and risk of Crohn's disease
    • doi:10.1002/ibd.21486
    • Henckaerts L, Cleynen I, Brinar M, John JM, Van Steen K, Rutgeerts P, et al. Genetic variation in the autophagy gene ULK1 and risk of Crohn's disease. Inflamm Bowel Dis (2011) 17(6):1392-7. doi:10.1002/ibd.21486.
    • (2011) Inflamm Bowel Dis , vol.17 , Issue.6 , pp. 1392-1397
    • Henckaerts, L.1    Cleynen, I.2    Brinar, M.3    John, J.M.4    Van Steen, K.5    Rutgeerts, P.6
  • 111
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • doi:10.1016/j.ceb.2009.11.014
    • Yang Z, Klionsky DJ. Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol (2010) 22(2):124-31. doi:10.1016/j.ceb.2009.11.014.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 112
    • 51649124519 scopus 로고    scopus 로고
    • Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation
    • doi:10.1182/blood-2008-02-137398
    • Kundu M, Lindsten T, Yang CY, Wu J, Zhao F, Zhang J, et al. Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood (2008) 112(4):1493-502. doi:10.1182/blood-2008-02-137398.
    • (2008) Blood , vol.112 , Issue.4 , pp. 1493-1502
    • Kundu, M.1    Lindsten, T.2    Yang, C.Y.3    Wu, J.4    Zhao, F.5    Zhang, J.6
  • 113
    • 78149473340 scopus 로고    scopus 로고
    • LRRK2 is involved in the IFN-gamma response and host response to pathogens
    • doi:10.4049/jimmunol.1000548
    • Gardet A, Benita Y, Li C, Sands BE, Ballester I, Stevens C, et al. LRRK2 is involved in the IFN-gamma response and host response to pathogens. J Immunol (2010) 185(9):5577-85. doi:10.4049/jimmunol.1000548.
    • (2010) J Immunol , vol.185 , Issue.9 , pp. 5577-5585
    • Gardet, A.1    Benita, Y.2    Li, C.3    Sands, B.E.4    Ballester, I.5    Stevens, C.6
  • 114
    • 84872517438 scopus 로고    scopus 로고
    • Distinct profiles of effector cytokines mark the different phases of Crohn's disease
    • doi:10.1371/journal.pone.0054562
    • Zorzi F, Monteleone I, Sarra M, Calabrese E, Marafini I, Cretella M, et al. Distinct profiles of effector cytokines mark the different phases of Crohn's disease. PLoS ONE (2013) 8(1):e54562. doi:10.1371/journal.pone.0054562.
    • (2013) PLoS ONE , vol.8 , Issue.1
    • Zorzi, F.1    Monteleone, I.2    Sarra, M.3    Calabrese, E.4    Marafini, I.5    Cretella, M.6
  • 115
    • 70349991886 scopus 로고    scopus 로고
    • LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model
    • doi:10.1093/hmg/ddp346
    • Alegre-Abarrategui J, Christian H, Lufino MM, Mutihac R, Venda LL, Ansorge O, et al. LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model. Hum Mol Genet (2009) 18(21):4022-34. doi:10.1093/hmg/ddp346.
    • (2009) Hum Mol Genet , vol.18 , Issue.21 , pp. 4022-4034
    • Alegre-Abarrategui, J.1    Christian, H.2    Lufino, M.M.3    Mutihac, R.4    Venda, L.L.5    Ansorge, O.6
  • 116
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • doi:10.1111/j.1471-4159.2008.05217.x
    • Plowey ED, Cherra SJ III, Liu YJ, Chu CT. Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells. J Neurochem (2008) 105(3):1048-56. doi:10.1111/j.1471-4159.2008.05217.x.
    • (2008) J Neurochem , vol.105 , Issue.3 , pp. 1048-1056
    • Plowey, E.D.1    Cherra I.I.I, S.J.2    Liu, Y.J.3    Chu, C.T.4
  • 117
    • 80054933395 scopus 로고    scopus 로고
    • The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease
    • doi:10.1038/ni.2113
    • Liu Z, Lee J, Krummey S, Lu W, Cai H, Lenardo MJ. The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease. Nat Immunol (2011) 12(11):1063-70. doi:10.1038/ni.2113.
    • (2011) Nat Immunol , vol.12 , Issue.11 , pp. 1063-1070
    • Liu, Z.1    Lee, J.2    Krummey, S.3    Lu, W.4    Cai, H.5    Lenardo, M.J.6
  • 118
    • 84862301902 scopus 로고    scopus 로고
    • Amino acid starvation induced by invasive bacterial pathogens triggers an innate host defense program
    • doi:10.1016/j.chom.2012.04.012
    • Tattoli I, Sorbara MT, Vuckovic D, Ling A, Soares F, Carneiro LA, et al. Amino acid starvation induced by invasive bacterial pathogens triggers an innate host defense program. Cell Host Microbe (2012) 11(6):563-75. doi:10.1016/j.chom.2012.04.012.
    • (2012) Cell Host Microbe , vol.11 , Issue.6 , pp. 563-575
    • Tattoli, I.1    Sorbara, M.T.2    Vuckovic, D.3    Ling, A.4    Soares, F.5    Carneiro, L.A.6
  • 119
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • doi:10.1074/jbc. M702824200
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem (2007) 282(33):24131-45. doi:10.1074/jbc. M702824200.
    • (2007) J Biol Chem , vol.282 , Issue.33 , pp. 24131-45
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6


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