메뉴 건너뛰기




Volumn 10, Issue 7, 2014, Pages 1154-1166

The autophagic roles of Rab small GTPases and their upstream regulators: A review

Author keywords

Autophagy; GAP; GEF; RAB; Small GTPases

Indexed keywords

RAB PROTEIN; RAB11 PROTEIN; RAB24 PROTEIN; RAB32 PROTEIN; RAB33 PROTEIN; RAB7 PROTEIN; RAB8 PROTEIN; RAB9 PROTEIN; UNCLASSIFIED DRUG;

EID: 84903836778     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.29395     Document Type: Review
Times cited : (122)

References (124)
  • 1
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • PMID:18191218
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132:27-42; PMID:18191218; http://dx.doi.org/10.1016/j.cell.2007.12.018
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 2
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • PMID:21801009
    • Mizushima N, Yoshimori T, Ohsumi Y. The role of Atg proteins in autophagosome formation. Annu Rev Cell Dev Biol 2011; 27:107-32; PMID:21801009; http://dx.doi.org/10.1146/annurev-cellbio-092910-154005
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 3
    • 79953153833 scopus 로고    scopus 로고
    • The late stage of autophagy: Cellular events and molecular regulation
    • PMID:21204017
    • Tong J, Yan X, Yu L. The late stage of autophagy: cellular events and molecular regulation. Protein Cell 2010; 1:907-15; PMID:21204017; http://dx.doi.org/10.1007/s13238-010-0121-z
    • (2010) Protein Cell , vol.1 , pp. 907-915
    • Tong, J.1    Yan, X.2    Yu, L.3
  • 4
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • PMID:19603039
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009; 10:513-25; PMID:19603039; http://dx.doi.org/10.1038/nrm2728
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 5
    • 77955239270 scopus 로고    scopus 로고
    • Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites
    • PMID:20545908
    • Zoppino FCM, Militello RD, Slavin I, Alvarez C, Colombo MI. Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites. Traffic 2010; 11:1246-61; PMID:20545908; http://dx.doi.org/10.1111/j.1600-0854. 2010.01086.x
    • (2010) Traffic , vol.11 , pp. 1246-1261
    • Zoppino, F.C.M.1    Militello, R.D.2    Slavin, I.3    Alvarez, C.4    Colombo, M.I.5
  • 7
    • 33845345128 scopus 로고    scopus 로고
    • Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae
    • PMID:16874038
    • Nazarko TY, Huang J, Nicaud JM, Klionsky DJ, Sibirny AA. Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae. Autophagy 2005; 1:37-45; PMID:16874038; http://dx.doi.org/10.4161/auto.1.1.1512
    • (2005) Autophagy , vol.1 , pp. 37-45
    • Nazarko, T.Y.1    Huang, J.2    Nicaud, J.M.3    Klionsky, D.J.4    Sibirny, A.A.5
  • 8
    • 25844489089 scopus 로고    scopus 로고
    • Trs85 (Gsg1), a component of the TRAPP complexes, is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway
    • PMID:16079147
    • Meiling-Wesse K, Epple UD, Krick R, Barth H, Appelles A, Voss C, Eskelinen E-L, Thumm M. Trs85 (Gsg1), a component of the TRAPP complexes, is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway. J Biol Chem 2005; 280:33669-78; PMID:16079147; http://dx.doi.org/10.1074/jbc.M501701200
    • (2005) J Biol Chem , vol.280 , pp. 33669-33678
    • Meiling-Wesse, K.1    Epple, U.D.2    Krick, R.3    Barth, H.4    Appelles, A.5    Voss, C.6    Eskelinen, E.-L.7    Thumm, M.8
  • 10
    • 84860797387 scopus 로고    scopus 로고
    • Regulation of selective autophagy onset by a Ypt/Rab GTPase module
    • PMID:22509044
    • Lipatova Z, Belogortseva N, Zhang XQ, Kim J, Taussig D, Segev N. Regulation of selective autophagy onset by a Ypt/Rab GTPase module. Proc Natl Acad Sci U S A 2012; 109:6981-6; PMID:22509044; http://dx.doi.org/10.1073/pnas. 1121299109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6981-6986
    • Lipatova, Z.1    Belogortseva, N.2    Zhang, X.Q.3    Kim, J.4    Taussig, D.5    Segev, N.6
  • 11
    • 75749135725 scopus 로고    scopus 로고
    • The conserved oligomeric Golgi complex is involved in dou-ble- membrane vesicle formation during autophagy
    • PMID:20065092
    • Yen W-L, Shintani T, Nair U, Cao Y, Richardson BC, Li Z, Hughson FM, Baba M, Klionsky DJ. The conserved oligomeric Golgi complex is involved in dou-ble- membrane vesicle formation during autophagy. J Cell Biol 2010; 188:101-14; PMID:20065092; http://dx.doi.org/10.1083/jcb.200904075
    • (2010) J Cell Biol , vol.188 , pp. 101-114
    • Yen, W.-L.1    Shintani, T.2    Nair, U.3    Cao, Y.4    Richardson, B.C.5    Li, Z.6    Hughson, F.M.7    Baba, M.8    Klionsky, D.J.9
  • 13
    • 46249127490 scopus 로고    scopus 로고
    • Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease
    • PMID:18430781
    • Ravikumar B, Imarisio S, Sarkar S, O'Kane CJ, Rubinsztein DC. Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease. J Cell Sci 2008; 121:1649-60; PMID:18430781; http://dx.doi.org/10.1242/jcs.025726
    • (2008) J Cell Sci , vol.121 , pp. 1649-1660
    • Ravikumar, B.1    Imarisio, S.2    Sarkar, S.3    O'Kane, C.J.4    Rubinsztein, D.C.5
  • 14
    • 80054978956 scopus 로고    scopus 로고
    • Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy
    • PMID:21835792
    • Su W-C, Chao T-C, Huang Y-L, Weng S-C, Jeng K-S, Lai MMC. Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. J Virol 2011; 85:10561-71; PMID:21835792; http://dx.doi.org/10.1128/JVI.00173-11
    • (2011) J Virol , vol.85 , pp. 10561-10571
    • Su, W.-C.1    Chao, T.-C.2    Huang, Y.-L.3    Weng, S.-C.4    Jeng, K.-S.5    Lai, M.M.C.6
  • 15
    • 78349244834 scopus 로고    scopus 로고
    • The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy
    • PMID:21059846
    • Dou Z, Chattopadhyay M, Pan J-A, Guerriero JL, Jiang Y-P, Ballou LM, Yue Z, Lin RZ, Zong W-X. The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy. J Cell Biol 2010; 191:827-43; PMID:21059846; http://dx.doi.org/10.1083/jcb.201006056
    • (2010) J Cell Biol , vol.191 , pp. 827-843
    • Dou, Z.1    Chattopadhyay, M.2    Pan, J.-A.3    Guerriero, J.L.4    Jiang, Y.-P.5    Ballou, L.M.6    Yue, Z.7    Lin, R.Z.8    Zong, W.-X.9
  • 16
    • 84876086849 scopus 로고    scopus 로고
    • Class IA PI3K p110β subunit promotes autophagy through Rab5 small GTPase in response to growth factor limitation
    • PMID:23434372
    • Dou Z, Pan J-A, Dbouk HA, Ballou LM, DeLeon JL, Fan Y, Chen J-S, Liang Z, Li G, Backer JM, et al. Class IA PI3K p110β subunit promotes autophagy through Rab5 small GTPase in response to growth factor limitation. Mol Cell 2013; 50:29-42; PMID:23434372; http://dx.doi.org/10.1016/j.molcel.2013.01.022
    • (2013) Mol Cell , vol.50 , pp. 29-42
    • Dou, Z.1    Pan, J.-A.2    Dbouk, H.A.3    Ballou, L.M.4    DeLeon, J.L.5    Fan, Y.6    Chen, J.-S.7    Liang, Z.8    Li, G.9    Backer, J.M.10
  • 17
    • 84862275111 scopus 로고    scopus 로고
    • Rab5 proteins regulate activation and localization of target of rapamycin complex 1
    • PMID:22547071
    • Bridges D, Fisher K, Zolov SN, Xiong T, Inoki K, Weisman LS, Saltiel AR. Rab5 proteins regulate activation and localization of target of rapamycin complex 1. J Biol Chem 2012; 287:20913-21; PMID:22547071; http://dx.doi.org/10. 1074/jbc.M111.334060
    • (2012) J Biol Chem , vol.287 , pp. 20913-20921
    • Bridges, D.1    Fisher, K.2    Zolov, S.N.3    Xiong, T.4    Inoki, K.5    Weisman, L.S.6    Saltiel, A.R.7
  • 18
    • 84896762116 scopus 로고    scopus 로고
    • HRES-1/Rab4 promotes the formation of LC3(+) autophagosomes and the accumulation of mitochondria during autophagy
    • PMID:24404161
    • Talaber G, Miklossy G, Oaks Z, Liu Y, Tooze SA, Chudakov DM, Banki K, Perl A. HRES-1/Rab4 promotes the formation of LC3(+) autophagosomes and the accumulation of mitochondria during autophagy. PLoS One 2014; 9:e84392; PMID:24404161; http://dx.doi.org/10.1371/journal.pone.0084392
    • (2014) PLoS One , vol.9
    • Talaber, G.1    Miklossy, G.2    Oaks, Z.3    Liu, Y.4    Tooze, S.A.5    Chudakov, D.M.6    Banki, K.7    Perl, A.8
  • 19
    • 78650687327 scopus 로고    scopus 로고
    • IGF-I stimulates Rab7-RILP interaction during neuronal autophagy
    • PMID:20849920
    • Bains M, Zaegel V, Mize-Berge J, Heidenreich KA. IGF-I stimulates Rab7-RILP interaction during neuronal autophagy. Neurosci Lett 2011; 488:112-7; PMID:20849920; http://dx.doi.org/10.1016/j.neulet.2010.09.018
    • (2011) Neurosci Lett , vol.488 , pp. 112-117
    • Bains, M.1    Zaegel, V.2    Mize-Berge, J.3    Heidenreich, K.A.4
  • 20
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • PMID:20100911
    • Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, Overvatn A, Bjørkøy G, Johansen T. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol 2010; 188:253-69; PMID:20100911; http://dx.doi.org/10.1083/jcb.200907015
    • (2010) J Cell Biol , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5    Overvatn, A.6    Bjørkøy, G.7    Johansen, T.8
  • 21
    • 84857858536 scopus 로고    scopus 로고
    • Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
    • PMID:22331844
    • Maday S, Wallace KE, Holzbaur ELF. Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. J Cell Biol 2012; 196:407-17; PMID:22331844; http://dx.doi.org/10.1083/jcb.201106120
    • (2012) J Cell Biol , vol.196 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.F.3
  • 22
    • 78650114245 scopus 로고    scopus 로고
    • Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway via a novel Rab7-binding domain
    • PMID:20943950
    • Tabata K, Matsunaga K, Sakane A, Sasaki T, Noda T, Yoshimori T. Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway via a novel Rab7-binding domain. Mol Biol Cell 2010; 21:4162-72; PMID:20943950; http://dx.doi.org/10.1091/mbc.E10-06-0495
    • (2010) Mol Biol Cell , vol.21 , pp. 4162-4172
    • Tabata, K.1    Matsunaga, K.2    Sakane, A.3    Sasaki, T.4    Noda, T.5    Yoshimori, T.6
  • 23
    • 78650600158 scopus 로고    scopus 로고
    • Rubicon controls endosome maturation as a Rab7 effector
    • PMID:20974968
    • Sun Q, Westphal W, Wong KN, Tan I, Zhong Q. Rubicon controls endosome maturation as a Rab7 effector. Proc Natl Acad Sci U S A 2010; 107:19338-43; PMID:20974968; http://dx.doi.org/10.1073/pnas.1010554107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19338-19343
    • Sun, Q.1    Westphal, W.2    Wong, K.N.3    Tan, I.4    Zhong, Q.5
  • 24
    • 84871903696 scopus 로고    scopus 로고
    • Maturation of autophagosomes and endosomes: A key role for Rab7
    • PMID:23220125
    • Hyttinen JMT, Niittykoski M, Salminen A, Kaarniranta K. Maturation of autophagosomes and endosomes: a key role for Rab7. Biochim Biophys Acta 2013; 1833:503-10; PMID:23220125; http://dx.doi.org/10.1016/j.bbamcr.2012.11.018
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 503-510
    • Hyttinen, J.M.T.1    Niittykoski, M.2    Salminen, A.3    Kaarniranta, K.4
  • 26
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • PMID:15138286
    • Gutierrez MG, Munafó DB, Berón W, Colombo MI. Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J Cell Sci 2004; 117:2687-97; PMID:15138286; http://dx.doi.org/10.1242/ jcs.01114
    • (2004) J Cell Sci , vol.117 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafó, D.B.2    Berón, W.3    Colombo, M.I.4
  • 28
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • PMID:17534139
    • Kimura S, Noda T, Yoshimori T. Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 2007; 3:452-60; PMID:17534139
    • (2007) Autophagy , vol.3 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 29
    • 80855148621 scopus 로고    scopus 로고
    • COP9 signalosome regulates autophagosome maturation
    • PMID:21986281
    • Su H, Li F, Ranek MJ, Wei N, Wang X. COP9 signalosome regulates autophagosome maturation. Circulation 2011; 124:2117-28; PMID:21986281; http://dx.doi.org/10.1161/CIRCULATIONAHA.111.048934
    • (2011) Circulation , vol.124 , pp. 2117-2128
    • Su, H.1    Li, F.2    Ranek, M.J.3    Wei, N.4    Wang, X.5
  • 30
    • 77949448601 scopus 로고    scopus 로고
    • Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes
    • PMID:20089838
    • Furuta N, Fujita N, Noda T, Yoshimori T, Amano A. Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes. Mol Biol Cell 2010; 21:1001-10; PMID:20089838; http://dx.doi.org/10. 1091/mbc.E09-08-0693
    • (2010) Mol Biol Cell , vol.21 , pp. 1001-1010
    • Furuta, N.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4    Amano, A.5
  • 31
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • PMID:21700220
    • Ganley IG, Wong P-M, Gammoh N, Jiang X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol Cell 2011; 42:731-43; PMID:21700220; http://dx.doi.org/10.1016/j.molcel.2011.04.024
    • (2011) Mol Cell , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.-M.2    Gammoh, N.3    Jiang, X.4
  • 32
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • PMID:20526321
    • Yu L, McPhee CK, Zheng L, Mardones GA, Rong Y, Peng J, Mi N, Zhao Y, Liu Z, Wan F, et al. Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 2010; 465:942-6; PMID:20526321; http://dx.doi.org/10.1038/ nature09076
    • (2010) Nature , vol.465 , pp. 942-946
    • Yu, L.1    McPhee, C.K.2    Zheng, L.3    Mardones, G.A.4    Rong, Y.5    Peng, J.6    Mi, N.7    Zhao, Y.8    Liu, Z.9    Wan, F.10
  • 34
    • 77954590749 scopus 로고    scopus 로고
    • Specific behavior of intracellular Streptococcus pyogenes that has undergone autophagic degradation is associated with bacterial streptolysin O and host small G proteins Rab5 and Rab7
    • PMID:20472552
    • Sakurai A, Maruyama F, Funao J, Nozawa T, Aikawa C, Okahashi N, Shintani S, Hamada S, Ooshima T, Nakagawa I. Specific behavior of intracellular Streptococcus pyogenes that has undergone autophagic degradation is associated with bacterial streptolysin O and host small G proteins Rab5 and Rab7. J Biol Chem 2010; 285:22666-75; PMID:20472552; http://dx.doi.org/10.1074/jbc.M109. 100131
    • (2010) J Biol Chem , vol.285 , pp. 22666-22675
    • Sakurai, A.1    Maruyama, F.2    Funao, J.3    Nozawa, T.4    Aikawa, C.5    Okahashi, N.6    Shintani, S.7    Hamada, S.8    Ooshima, T.9    Nakagawa, I.10
  • 35
    • 73549102459 scopus 로고    scopus 로고
    • An initial step of GAScontaining autophagosome-like vacuoles formation requires Rab7
    • PMID:19956673
    • Yamaguchi H, Nakagawa I, Yamamoto A, Amano A, Noda T, Yoshimori T. An initial step of GAScontaining autophagosome-like vacuoles formation requires Rab7. PLoS Pathog 2009; 5:e1000670; PMID:19956673; http://dx.doi.org/10.1371/ journal.ppat.1000670
    • (2009) PLoS Pathog , vol.5
    • Yamaguchi, H.1    Nakagawa, I.2    Yamamoto, A.3    Amano, A.4    Noda, T.5    Yoshimori, T.6
  • 36
    • 77649140362 scopus 로고    scopus 로고
    • The late endosome is essential for mTORC1 signaling
    • PMID:20053679
    • Flinn RJ, Yan Y, Goswami S, Parker PJ, Backer JM. The late endosome is essential for mTORC1 signaling. Mol Biol Cell 2010; 21:833-41; PMID:20053679; http://dx.doi.org/10.1091/mbc.E09-09-0756
    • (2010) Mol Biol Cell , vol.21 , pp. 833-841
    • Flinn, R.J.1    Yan, Y.2    Goswami, S.3    Parker, P.J.4    Backer, J.M.5
  • 37
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β
    • PMID:22068051
    • Dupont N, Jiang S, Pilli M, Ornatowski W, Bhattacharya D, Deretic V. Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β. EMBO J 2011; 30:4701-11; PMID:22068051; http://dx.doi.org/10.1038/ emboj.2011.398
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 39
    • 84864009466 scopus 로고    scopus 로고
    • The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during Group A Streptococcus infection
    • PMID:22452336
    • Nozawa T, Aikawa C, Goda A, Maruyama F, Hamada S, Nakagawa I. The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during Group A Streptococcus infection. Cell Microbiol 2012; 14:1149-65; PMID:22452336; http://dx.doi.org/10.1111/j.1462-5822.2012.01792.x
    • (2012) Cell Microbiol , vol.14 , pp. 1149-1165
    • Nozawa, T.1    Aikawa, C.2    Goda, A.3    Maruyama, F.4    Hamada, S.5    Nakagawa, I.6
  • 41
    • 84862611041 scopus 로고    scopus 로고
    • TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
    • PMID:22613832
    • Longatti A, Lamb CA, Razi M, Yoshimura S, Barr FA, Tooze SA. TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes. J Cell Biol 2012; 197:659-75; PMID:22613832; http://dx.doi.org/10. 1083/jcb.201111079
    • (2012) J Cell Biol , vol.197 , pp. 659-675
    • Longatti, A.1    Lamb, C.A.2    Razi, M.3    Yoshimura, S.4    Barr, F.A.5    Tooze, S.A.6
  • 43
    • 84884220705 scopus 로고    scopus 로고
    • Diverse autophagosome membrane sources coalesce in recycling endosomes
    • PMID:24034251
    • Puri C, Renna M, Bento CF, Moreau K, Rubinsztein DC. Diverse autophagosome membrane sources coalesce in recycling endosomes. Cell 2013; 154:1285-99; PMID:24034251; http://dx.doi.org/10.1016/j.cell.2013.08.044
    • (2013) Cell , vol.154 , pp. 1285-1299
    • Puri, C.1    Renna, M.2    Bento, C.F.3    Moreau, K.4    Rubinsztein, D.C.5
  • 44
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • PMID:17999726
    • Fader CM, Sánchez D, Furlán M, Colombo MI. Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells. Traffic 2008; 9:230-50; PMID:17999726; http://dx.doi.org/10.1111/j. 1600-0854.2007.00677.x
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.M.1    Sánchez, D.2    Furlán, M.3    Colombo, M.I.4
  • 45
    • 72049088519 scopus 로고    scopus 로고
    • TI-VAMP/VAMP7 and VAMP3/cellubrevin: Two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways
    • PMID:19781582
    • Fader CM, Sánchez DG, Mestre MB, Colombo MI. TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways. Biochim Biophys Acta 2009; 1793:1901-16; PMID:19781582; http://dx.doi.org/10.1016/j.bbamcr.2009.09.011
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1901-1916
    • Fader, C.M.1    Sánchez, D.G.2    Mestre, M.B.3    Colombo, M.I.4
  • 47
    • 84894275180 scopus 로고    scopus 로고
    • Rab11 facilitates cross-talk between autophagy and endosomal pathway through regulation of Hook localization
    • PMID:24356450
    • Szatmári Z, Kis V, Lippai M, Hegedus K, Faragó T, Lorincz P, Tanaka T, Juhász G, Sass M. Rab11 facilitates cross-talk between autophagy and endosomal pathway through regulation of Hook localization. Mol Biol Cell 2014; 25:522-31; PMID:24356450; http://dx.doi.org/10.1091/mbc.E13-10- 0574
    • (2014) Mol Biol Cell , vol.25 , pp. 522-531
    • Szatmári, Z.1    Kis, V.2    Lippai, M.3    Hegedus, K.4    Faragó, T.5    Lorincz, P.6    Tanaka, T.7    Juhász, G.8    Sass, M.9
  • 48
    • 0036017758 scopus 로고    scopus 로고
    • Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24
    • PMID:12047555
    • Munafó DB, Colombo MI. Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24. Traffic 2002; 3:472-82; PMID:12047555; http://dx.doi.org/10.1034/j.1600-0854.2002.30704.x
    • (2002) Traffic , vol.3 , pp. 472-482
    • Munafó, D.B.1    Colombo, M.I.2
  • 49
    • 68949214328 scopus 로고    scopus 로고
    • A small GTPase, human Rab32, is required for the formation of autophagic vacuoles under basal conditions
    • PMID:19593531
    • Hirota Y, Tanaka Y. A small GTPase, human Rab32, is required for the formation of autophagic vacuoles under basal conditions. Cell Mol Life Sci 2009; 66:2913-32; PMID:19593531; http://dx.doi.org/10.1007/s00018-009-0080-9
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2913-2932
    • Hirota, Y.1    Tanaka, Y.2
  • 51
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • PMID:18448665
    • Itoh T, Fujita N, Kanno E, Yamamoto A, Yoshimori T, Fukuda M. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol Biol Cell 2008; 19:2916-25; PMID:18448665; 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
  • 52
    • 79952422876 scopus 로고    scopus 로고
    • OATL1, a novel autophagosome-resident Rab33BGAP, regulates autophagosomal maturation
    • PMID:21383079
    • Itoh T, Kanno E, Uemura T, Waguri S, Fukuda M. OATL1, a novel autophagosome-resident Rab33BGAP, regulates autophagosomal maturation. J Cell Biol 2011; 192:839-53; PMID:21383079; http://dx.doi.org/10.1083/jcb.201008107
    • (2011) J Cell Biol , vol.192 , pp. 839-853
    • Itoh, T.1    Kanno, E.2    Uemura, T.3    Waguri, S.4    Fukuda, M.5
  • 53
    • 84903823741 scopus 로고    scopus 로고
    • Endocytic Rabs in membrane trafficking and signaling
    • PMID:24158421
    • Numrich J, Ungermann C. Endocytic Rabs in membrane trafficking and signaling. Biol Chem 2014; 395:327-33; PMID:24158421; http://dx.doi.org/10.1515/ hsz-2013-0258
    • (2014) Biol Chem , vol.395 , pp. 327-333
    • Numrich, J.1    Ungermann, C.2
  • 54
    • 0036300306 scopus 로고    scopus 로고
    • Role of Rab5 in the recruitment of hVps34/p150 to the early endosome
    • PMID:12010460
    • Murray JT, Panaretou C, Stenmark H, Miaczynska M, Backer JM. Role of Rab5 in the recruitment of hVps34/p150 to the early endosome. Traffic 2002; 3:416-27; PMID:12010460; http://dx.doi.org/10.1034/j.1600-0854.2002.30605.x
    • (2002) Traffic , vol.3 , pp. 416-427
    • Murray, J.T.1    Panaretou, C.2    Stenmark, H.3    Miaczynska, M.4    Backer, J.M.5
  • 55
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
    • PMID:1516131
    • van der Sluijs P, Hull M, Webster P, Mâle P, Goud B, Mellman I. The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell 1992; 70:729-40; PMID:1516131; http://dx.doi.org/10.1016/0092- 8674(92)90307-X
    • (1992) Cell , vol.70 , pp. 729-740
    • Van Der Sluijs, P.1    Hull, M.2    Webster, P.3    Mâle, P.4    Goud, B.5    Mellman, I.6
  • 56
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • PMID:10811830
    • Sönnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 2000; 149:901-14; PMID:10811830; http://dx.doi.org/10.1083/jcb.149.4.901
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sönnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 57
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • PMID:21878991
    • Huotari J, Helenius A. Endosome maturation. EMBO J 2011; 30:3481-500; PMID:21878991; http://dx.doi.org/10.1038/emboj.2011.286
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 58
    • 78650419576 scopus 로고    scopus 로고
    • Rab7: Role of its protein interaction cascades in endolysosomal traffic
    • PMID:20851765
    • Wang T, Ming Z, Xiaochun W, Hong W. Rab7: role of its protein interaction cascades in endolysosomal traffic. Cell Signal 2011; 23:516-21; PMID:20851765; http://dx.doi.org/10.1016/j.cellsig.2010.09.012
    • (2011) Cell Signal , vol.23 , pp. 516-521
    • Wang, T.1    Ming, Z.2    Xiaochun, W.3    Hong, W.4
  • 59
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • PMID:16176980
    • Johansson M, Lehto M, Tanhuanpää K, Cover TL, Olkkonen VM. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell 2005; 16:5480-92; PMID:16176980; http://dx.doi.org/10.1091/mbc.E05-03-0189
    • (2005) Mol Biol Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpää, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 60
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
    • PMID:17283181
    • Johansson M, Rocha N, Zwart W, Jordens I, Janssen L, Kuijl C, Olkkonen VM, Neefjes J. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J Cell Biol 2007; 176:459-71; PMID:17283181; http://dx.doi.org/10.1083/jcb.200606077
    • (2007) J Cell Biol , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5    Kuijl, C.6    Olkkonen, V.M.7    Neefjes, J.8
  • 61
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • PMID:11696325
    • Jordens I, Fernandez-Borja M, Marsman M, Dusseljee S, Janssen L, Calafat J, Janssen H, Wubbolts R, Neefjes J. The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr Biol 2001; 11:1680-5; PMID:11696325; http://dx.doi.org/10.1016/S0960-9822(01) 00531-0
    • (2001) Curr Biol , vol.11 , pp. 1680-1685
    • Jordens, I.1    Fernandez-Borja, M.2    Marsman, M.3    Dusseljee, S.4    Janssen, L.5    Calafat, J.6    Janssen, H.7    Wubbolts, R.8    Neefjes, J.9
  • 62
    • 0035800740 scopus 로고    scopus 로고
    • Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7
    • PMID:11382755
    • Kim BY, Krämer H, Yamamoto A, Kominami E, Kohsaka S, Akazawa C. Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7. J Biol Chem 2001; 276:29393-402; PMID:11382755; http://dx.doi.org/10.1074/jbc.M101778200
    • (2001) J Biol Chem , vol.276 , pp. 29393-29402
    • Kim, B.Y.1    Krämer, H.2    Yamamoto, A.3    Kominami, E.4    Kohsaka, S.5    Akazawa, C.6
  • 63
    • 48749099702 scopus 로고    scopus 로고
    • HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
    • PMID:18385512
    • Starai VJ, Hickey CM, Wickner W. HOPS proofreads the trans-SNARE complex for yeast vacuole fusion. Mol Biol Cell 2008; 19:2500-8; PMID:18385512; http://dx.doi.org/10.1091/mbc.E08-01-0077
    • (2008) Mol Biol Cell , vol.19 , pp. 2500-2508
    • Starai, V.J.1    Hickey, C.M.2    Wickner, W.3
  • 64
    • 0141744731 scopus 로고    scopus 로고
    • Rabring7, a novel Rab7 target protein with a RING finger motif
    • PMID:12972561
    • Mizuno K, Kitamura A, Sasaki T. Rabring7, a novel Rab7 target protein with a RING finger motif. Mol Biol Cell 2003; 14:3741-52; PMID:12972561; http://dx.doi.org/10.1091/mbc.E02-08-0495
    • (2003) Mol Biol Cell , vol.14 , pp. 3741-3752
    • Mizuno, K.1    Kitamura, A.2    Sasaki, T.3
  • 65
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • PMID:18552835
    • Liang C, Lee JS, Inn KS, Gack MU, Li Q, Roberts EA, Vergne I, Deretic V, Feng P, Akazawa C, et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat Cell Biol 2008; 10:776-87; PMID:18552835; http://dx.doi.org/10.1038/ncb1740
    • (2008) Nat Cell Biol , vol.10 , 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
  • 67
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • PMID:19270693
    • Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, Heintz N, Yue Z. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol 2009; 11:468-76; PMID:19270693; http://dx.doi.org/10.1038/ncb1854
    • (2009) Nat Cell Biol , vol.11 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6    Heintz, N.7    Yue, Z.8
  • 68
    • 79956057019 scopus 로고    scopus 로고
    • Interaction between small GTPase Rab7 and PI3KC3 links autophagy and endocytosis: A new Rab7 effector protein sheds light on membrane trafficking pathways
    • PMID:21776407
    • Lin MG, Zhong Q. Interaction between small GTPase Rab7 and PI3KC3 links autophagy and endocytosis: A new Rab7 effector protein sheds light on membrane trafficking pathways. Small GTPases 2011; 2:85-8; PMID:21776407; http://dx.doi.org/10.4161/sgtp.2.2.15256
    • (2011) Small GTPases , vol.2 , pp. 85-88
    • Lin, M.G.1    Zhong, Q.2
  • 69
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • PMID:19364919
    • Razi M, Chan EYW, Tooze SA. Early endosomes and endosomal coatomer are required for autophagy. J Cell Biol 2009; 185:305-21; PMID:19364919; http://dx.doi.org/10.1083/jcb.200810098
    • (2009) J Cell Biol , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.W.2    Tooze, S.A.3
  • 70
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes
    • PMID:16420522
    • Köchl R, Hu XW, Chan EYW, Tooze SA. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic 2006; 7:129-45; PMID:16420522; http://dx.doi.org/10.1111/j.1600-0854.2005.00368. x
    • (2006) Traffic , vol.7 , pp. 129-145
    • Köchl, R.1    Hu, X.W.2    Chan, E.Y.W.3    Tooze, S.A.4
  • 71
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • PMID:17984323
    • Filimonenko M, Stuffers S, Raiborg C, Yamamoto A, Malerød L, Fisher EMC, Isaacs A, Brech A, Stenmark H, Simonsen A. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol 2007; 179:485-500; PMID:17984323; http://dx.doi.org/10.1083/jcb.200702115
    • (2007) J Cell Biol , vol.179 , pp. 485-500
    • Filimonenko, M.1    Stuffers, S.2    Raiborg, C.3    Yamamoto, A.4    Malerød, L.5    Fisher, E.M.C.6    Isaacs, A.7    Brech, A.8    Stenmark, H.9    Simonsen, A.10
  • 72
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • PMID:3126737
    • Gordon PB, Seglen PO. Prelysosomal convergence of autophagic and endocytic pathways. Biochem Biophys Res Commun 1988; 151:40-7; PMID:3126737; http://dx.doi.org/10.1016/0006-291X(88)90556-6
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 73
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • PMID:23217709
    • 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; 151:1256-69; PMID:23217709; http://dx.doi.org/10.1016/j.cell.2012. 11.001
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 74
    • 84878615771 scopus 로고    scopus 로고
    • Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila
    • PMID:23671310
    • Takáts S, Nagy P, Varga Á, Pircs K, Kárpáti M, Varga K, Kovács AL, Hegedu{combining double acute accent}s K, Juhász G. Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila. J Cell Biol 2013; 201:531-9; PMID:23671310; http://dx.doi.org/10.1083/jcb.201211160
    • (2013) J Cell Biol , vol.201 , pp. 531-539
    • Takáts, S.1    Nagy, P.2    Varga, Á.3    Pircs, K.4    Kárpáti, M.5    Varga, K.6    Kovács, A.L.7    Hegedus, K.8    Juhász, G.9
  • 75
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • PMID:18670193
    • Díaz-Troya S, Pérez-Pérez ME, Florencio FJ, Crespo JL. The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy 2008; 4:851-65; PMID:18670193
    • (2008) Autophagy , vol.4 , pp. 851-865
    • Díaz-Troya, S.1    Pérez-Pérez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 76
    • 84875423993 scopus 로고    scopus 로고
    • Amino acid signalling upstream of mTOR
    • PMID:23361334
    • Jewell JL, Russell RC, Guan K-L. Amino acid signalling upstream of mTOR. Nat Rev Mol Cell Biol 2013; 14:133-9; PMID:23361334; http://dx.doi.org/10.1038/ nrm3522
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 133-139
    • Jewell, J.L.1    Russell, R.C.2    Guan, K.-L.3
  • 77
    • 79960679137 scopus 로고    scopus 로고
    • Disruption of endocytic pathway regulatory genes activates autophagy in C. elegans
    • PMID:21618079
    • Dwivedi M, Sung H, Shen H, Park B-J, Lee S. Disruption of endocytic pathway regulatory genes activates autophagy in C. elegans. Mol Cells 2011; 31:477-81; PMID:21618079; http://dx.doi.org/10.1007/s10059-011-1035-1
    • (2011) Mol Cells , vol.31 , pp. 477-481
    • Dwivedi, M.1    Sung, H.2    Shen, H.3    Park, B.-J.4    Lee, S.5
  • 78
    • 79952317005 scopus 로고    scopus 로고
    • Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation
    • PMID:21300063
    • Otomo A, Kunita R, Suzuki-Utsunomiya K, Ikeda J-E, Hadano S. Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation. FEBS Lett 2011; 585:730-6; PMID:21300063; http://dx.doi.org/10.1016/ j.febslet.2011.01.045
    • (2011) FEBS Lett , vol.585 , pp. 730-736
    • Otomo, A.1    Kunita, R.2    Suzuki-Utsunomiya, K.3    Ikeda, J.-E.4    Hadano, S.5
  • 79
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis - Golgi tethering
    • PMID:11285137
    • Moyer BD, Allan BB, Balch WE. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis - Golgi tethering. Traffic 2001; 2:268-76; PMID:11285137; http://dx.doi.org/10.1034/j.1600-0854.2001.1o007.x
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 80
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • PMID:18725538
    • Axe EL, Walker SA, Manifava M, Chandra P, Roderick HL, Habermann A, Griffiths G, Ktistakis NT. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 2008; 182:685-701; PMID:18725538; http://dx.doi.org/10.1083/jcb.200803137
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 81
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • PMID:19898463
    • 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; 11:1433-7; PMID:19898463; http://dx.doi.org/10. 1038/ncb1991
    • (2009) Nat Cell Biol , vol.11 , pp. 1433-1437
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3    Yamaguchi, A.4    Yoshimori, T.5    Yamamoto, A.6
  • 82
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • PMID:19855179
    • Ylä-Anttila P, Vihinen H, Jokitalo E, Eskelinen E-L. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 2009; 5:1180-5; PMID:19855179; http://dx.doi.org/10.4161/auto.5.8.10274
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Ylä-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.-L.4
  • 83
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • PMID:20639694
    • Itakura E, Mizushima N. Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 2010; 6:764-76; PMID:20639694; http://dx.doi.org/10.4161/auto.6.6.12709
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 84
    • 84871581862 scopus 로고    scopus 로고
    • Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    • PMID:23219485
    • Ragusa MJ, Stanley RE, Hurley JH. Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell 2012; 151:1501-12; PMID:23219485; http://dx.doi.org/10.1016/j.cell.2012.11.028
    • (2012) Cell , vol.151 , pp. 1501-1512
    • Ragusa, M.J.1    Stanley, R.E.2    Hurley, J.H.3
  • 85
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • PMID:20855505
    • 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; 190:1005-22; PMID:20855505; http://dx.doi.org/10. 1083/jcb.200912089
    • (2010) J Cell Biol , vol.190 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krishnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 88
    • 33845692364 scopus 로고    scopus 로고
    • Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast
    • PMID:17178909
    • He C, Song H, Yorimitsu T, Monastyrska I, Yen W-L, Legakis JE, Klionsky DJ. Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast. J Cell Biol 2006; 175:925-35; PMID:17178909; http://dx.doi.org/10.1083/jcb.200606084
    • (2006) J Cell Biol , vol.175 , pp. 925-935
    • He, C.1    Song, H.2    Yorimitsu, T.3    Monastyrska, I.4    Yen, W.-L.5    Legakis, J.E.6    Klionsky, D.J.7
  • 89
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • PMID:12011112
    • Suvorova ES, Duden R, Lupashin VV. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol 2002; 157:631-43; PMID:12011112; http://dx.doi.org/10.1083/jcb.200111081
    • (2002) J Cell Biol , vol.157 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 93
    • 77955051719 scopus 로고    scopus 로고
    • Transport at the recycling endosome
    • PMID:20541925
    • Hsu VW, Prekeris R. Transport at the recycling endosome. Curr Opin Cell Biol 2010; 22:528-34; PMID:20541925; http://dx.doi.org/10.1016/j.ceb.2010.05.008
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 528-534
    • Hsu, V.W.1    Prekeris, R.2
  • 94
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • PMID:11102533
    • Jones S, Newman C, Liu F, Segev N. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell 2000; 11:4403-11; PMID:11102533; http://dx.doi.org/10.1091/mbc.11.12.4403
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 97
    • 70149084564 scopus 로고    scopus 로고
    • A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway
    • PMID:19666511
    • Rivera-Molina FE, Novick PJ. A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway. Proc Natl Acad Sci U S A 2009; 106:14408-13; PMID:19666511; http://dx.doi.org/10.1073/pnas.0906536106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14408-14413
    • Rivera-Molina, F.E.1    Novick, P.J.2
  • 98
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • PMID:11827983
    • Barbero P, Bittova L, Pfeffer SR. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol 2002; 156:511-8; PMID:11827983; http://dx.doi.org/10.1083/jcb.200109030
    • (2002) J Cell Biol , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 99
    • 77958471298 scopus 로고    scopus 로고
    • Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
    • PMID:20937701
    • Yoshimura S, Gerondopoulos A, Linford A, Rigden DJ, Barr FA. Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors. J Cell Biol 2010; 191:367-81; PMID:20937701; http://dx.doi.org/10.1083/jcb.201008051
    • (2010) J Cell Biol , vol.191 , pp. 367-381
    • Yoshimura, S.1    Gerondopoulos, A.2    Linford, A.3    Rigden, D.J.4    Barr, F.A.5
  • 100
    • 0035900422 scopus 로고    scopus 로고
    • Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER
    • PMID:11718716
    • Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T. Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. FEBS Lett 2001; 508:201-9; PMID:11718716; http://dx.doi.org/10.1016/S0014- 5793(01)02993-3
    • (2001) FEBS Lett , vol.508 , pp. 201-209
    • Valsdottir, R.1    Hashimoto, H.2    Ashman, K.3    Koda, T.4    Storrie, B.5    Nilsson, T.6
  • 102
    • 48249101885 scopus 로고    scopus 로고
    • Rab8 regulates basolateral secretory, but not recycling, traffic at the recycling endosome
    • PMID:18287531
    • Henry L, Sheff DR. Rab8 regulates basolateral secretory, but not recycling, traffic at the recycling endosome. Mol Biol Cell 2008; 19:2059-68; PMID:18287531; http://dx.doi.org/10.1091/mbc.E07-09-0902
    • (2008) Mol Biol Cell , vol.19 , pp. 2059-2068
    • Henry, L.1    Sheff, D.R.2
  • 103
    • 34547810829 scopus 로고    scopus 로고
    • Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3
    • PMID:17507647
    • Roland JT, Kenworthy AK, Peranen J, Caplan S, Goldenring JR. Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. Mol Biol Cell 2007; 18:2828-37; PMID:17507647; http://dx.doi.org/10.1091/mbc.E07-02-0169
    • (2007) Mol Biol Cell , vol.18 , pp. 2828-2837
    • Roland, J.T.1    Kenworthy, A.K.2    Peranen, J.3    Caplan, S.4    Goldenring, J.R.5
  • 104
    • 0027743432 scopus 로고
    • Molecular cloning and subcellular localization of three GTP-binding proteins of the rab subfamily
    • PMID:8126105
    • Olkkonen VM, Dupree P, Killisch I, Lütcke A, Zerial M, Simons K. Molecular cloning and subcellular localization of three GTP-binding proteins of the rab subfamily. J Cell Sci 1993; 106:1249-61; PMID:8126105
    • (1993) J Cell Sci , vol.106 , pp. 1249-1261
    • Olkkonen, V.M.1    Dupree, P.2    Killisch, I.3    Lütcke, A.4    Zerial, M.5    Simons, K.6
  • 105
    • 85046983921 scopus 로고    scopus 로고
    • Cell type-specific Rab32 and Rab38 cooperate with the ubiquitous lysosome biogenesis machinery to synthesize specialized lysosome-related organelles
    • PMID:23247405
    • Bultema JJ, Di Pietro SM. Cell type-specific Rab32 and Rab38 cooperate with the ubiquitous lysosome biogenesis machinery to synthesize specialized lysosome-related organelles. Small GTPases 2013; 4:16-21; PMID:23247405; http://dx.doi.org/10.4161/sgtp.22349
    • (2013) Small GTPases , vol.4 , pp. 16-21
    • Bultema, J.J.1    Di Pietro, S.M.2
  • 108
    • 80054758176 scopus 로고    scopus 로고
    • Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation
    • PMID:21687989
    • Chua CEL, Gan BQ, Tang BL. Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation. Cell Mol Life Sci 2011; 68:3349-58; PMID:21687989; http://dx.doi.org/10.1007/s00018-011-0748-9
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3349-3358
    • Chua, C.E.L.1    Gan, B.Q.2    Tang, B.L.3
  • 114
    • 77950682093 scopus 로고    scopus 로고
    • Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease
    • PMID:20357106
    • Li X, Valencia A, Sapp E, Masso N, Alexander J, Reeves P, Kegel KB, Aronin N, Difiglia M. Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease. J Neurosci 2010; 30:4552-61; PMID:20357106; http://dx.doi.org/10.1523/JNEUROSCI.5865-09.2010
    • (2010) J Neurosci , vol.30 , pp. 4552-4561
    • Li, X.1    Valencia, A.2    Sapp, E.3    Masso, N.4    Alexander, J.5    Reeves, P.6    Kegel, K.B.7    Aronin, N.8    Difiglia, M.9
  • 115
    • 84861224193 scopus 로고    scopus 로고
    • Deficient Rab11 activity underlies glucose hypometabolism in primary neurons of Huntington's disease mice
    • PMID:22542623
    • Li X, Valencia A, McClory H, Sapp E, Kegel KB, Difiglia M. Deficient Rab11 activity underlies glucose hypometabolism in primary neurons of Huntington's disease mice. Biochem Biophys Res Commun 2012; 421:727-30; PMID:22542623; http://dx.doi.org/10.1016/j.bbrc.2012.04.070
    • (2012) Biochem Biophys Res Commun , vol.421 , pp. 727-730
    • Li, X.1    Valencia, A.2    McClory, H.3    Sapp, E.4    Kegel, K.B.5    Difiglia, M.6
  • 116
    • 84863518971 scopus 로고    scopus 로고
    • Rab11 rescues synaptic dysfunction and behavioural deficits in a Drosophila model of Huntington's disease
    • PMID:22466800
    • Steinert JR, Campesan S, Richards P, Kyriacou CP, Forsythe ID, Giorgini F. Rab11 rescues synaptic dysfunction and behavioural deficits in a Drosophila model of Huntington's disease. Hum Mol Genet 2012; 21:2912-22; PMID:22466800; http://dx.doi.org/10.1093/hmg/dds117
    • (2012) Hum Mol Genet , vol.21 , pp. 2912-2922
    • Steinert, J.R.1    Campesan, S.2    Richards, P.3    Kyriacou, C.P.4    Forsythe, I.D.5    Giorgini, F.6
  • 119
    • 36148991943 scopus 로고    scopus 로고
    • Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease
    • PMID:16103921
    • Ko DC, Milenkovic L, Beier SM, Manuel H, Buchanan J, Scott MP. Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease. PLoS Genet 2005; 1:81-95; PMID:16103921
    • (2005) PLoS Genet , vol.1 , pp. 81-95
    • Ko, D.C.1    Milenkovic, L.2    Beier, S.M.3    Manuel, H.4    Buchanan, J.5    Scott, M.P.6
  • 123
    • 58249095949 scopus 로고    scopus 로고
    • Development of a Rab9 transgenic mouse and its ability to increase the lifespan of a murine model of Niemann-Pick type C disease
    • PMID:19056848
    • Kaptzan T, West SA, Holicky EL, Wheatley CL, Marks DL, Wang T, Peake KB, Vance J, Walkley SU, Pagano RE. Development of a Rab9 transgenic mouse and its ability to increase the lifespan of a murine model of Niemann-Pick type C disease. Am J Pathol 2009; 174:14-20; PMID:19056848; http://dx.doi.org/10.2353/ ajpath.2009.080660
    • (2009) Am J Pathol , vol.174 , pp. 14-20
    • Kaptzan, T.1    West, S.A.2    Holicky, E.L.3    Wheatley, C.L.4    Marks, D.L.5    Wang, T.6    Peake, K.B.7    Vance, J.8    Walkley, S.U.9    Pagano, R.E.10
  • 124
    • 84861396483 scopus 로고    scopus 로고
    • Rab GTPase-activating proteins in autophagy: Regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers
    • PMID:22354992
    • Popovic D, Akutsu M, Novak I, Harper JW, Behrends C, Dikic I. Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers. Mol Cell Biol 2012; 32:1733-44; PMID:22354992; http://dx.doi.org/10.1128/MCB.06717-11
    • (2012) Mol Cell Biol , vol.32 , pp. 1733-1744
    • Popovic, D.1    Akutsu, M.2    Novak, I.3    Harper, J.W.4    Behrends, C.5    Dikic, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.