메뉴 건너뛰기




Volumn 68, Issue 20, 2011, Pages 3349-3358

Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation

Author keywords

Autophagosome; Autophagy; Parkinson's disease; Rab; RalB

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PROTEIN YPT1; RAB PROTEIN; RAB24 PROTEIN; RAB33 PROTEIN; RAB9 PROTEIN; RAL PROTEIN; RALA PROTEIN; RALB PROTEIN; UNCLASSIFIED DRUG;

EID: 80054758176     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-011-0748-9     Document Type: Review
Times cited : (109)

References (93)
  • 1
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • DOI 10.1126/science.290.5497.1717
    • DJ Klionsky SD Emr 2000 Autophagy as a regulated pathway of cellular degradation Science 290 1717 1721 11099404 10.1126/science.290.5497.1717 1:CAS:528:DC%2BD3cXovVOitbw%3D (Pubitemid 32004796)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 2
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macroautophagy
    • 20811353 10.1038/ncb0910-814 1:CAS:528:DC%2BC3cXhtFSju7zE
    • Z Yang DJ Klionsky 2010 Eaten alive: a history of macroautophagy Nat Cell Biol 12 814 822 20811353 10.1038/ncb0910-814 1:CAS:528:DC%2BC3cXhtFSju7zE
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 3
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • 20965422 10.1016/j.molcel.2010.09.023 1:CAS:528:DC%2BC3cXhtlCjtr%2FM
    • G Kroemer G Mariño B Levine 2010 Autophagy and the integrated stress response Mol cell 40 280 293 20965422 10.1016/j.molcel.2010.09.023 1:CAS:528:DC%2BC3cXhtlCjtr%2FM
    • (2010) Mol Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 4
    • 79954417611 scopus 로고    scopus 로고
    • Autophagy for tissue homeostasis and neuroprotection
    • Mariño G, Madeo F, Kroemer G (2010) Autophagy for tissue homeostasis and neuroprotection. Curr Opin Cell Biol 23:198-206
    • (2010) Curr Opin Cell Biol , vol.23 , pp. 198-206
    • Mariño, G.1    Madeo, F.2    Kroemer, G.3
  • 5
    • 78149471570 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disorders: Pathogenic roles and therapeutic implications
    • 20947179 10.1016/j.tins.2010.09.001 1:CAS:528:DC%2BC3cXhsVagurjF
    • R Banerjee MF Beal B Thomas 2010 Autophagy in neurodegenerative disorders: pathogenic roles and therapeutic implications Trends Neurosci 33 541 549 20947179 10.1016/j.tins.2010.09.001 1:CAS:528:DC%2BC3cXhsVagurjF
    • (2010) Trends Neurosci , vol.33 , pp. 541-549
    • Banerjee, R.1    Beal, M.F.2    Thomas, B.3
  • 6
    • 78649299872 scopus 로고    scopus 로고
    • Autophagy in the central nervous system: Implications for neurodegenerative disorders
    • 20942791 1:CAS:528:DC%2BC3cXhsFarsb3I
    • M Xilouri L Stefanis 2010 Autophagy in the central nervous system: implications for neurodegenerative disorders CNS Neurol Disord Drug Targets 9 701 719 20942791 1:CAS:528:DC%2BC3cXhsFarsb3I
    • (2010) CNS Neurol Disord Drug Targets , vol.9 , pp. 701-719
    • Xilouri, M.1    Stefanis, L.2
  • 7
    • 79952100709 scopus 로고    scopus 로고
    • Autophagosomes and human diseases
    • 21256243 10.1016/j.biocel.2011.01.006 1:CAS:528:DC%2BC3MXisFGmt7k%3D
    • I Beau M Mehrpour P Codogno 2011 Autophagosomes and human diseases Int J Biochem Cell Biol 43 460 464 21256243 10.1016/j.biocel.2011.01.006 1:CAS:528:DC%2BC3MXisFGmt7k%3D
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 460-464
    • Beau, I.1    Mehrpour, M.2    Codogno, P.3
  • 8
    • 79551634458 scopus 로고    scopus 로고
    • Autophagy in tumorigenesis and energy metabolism: Friend by day, foe by night
    • 21255998 10.1016/j.gde.2010.12.008 1:CAS:528:DC%2BC3MXhvFKjtLc%3D
    • R Mathew E White 2011 Autophagy in tumorigenesis and energy metabolism: friend by day, foe by night Curr Opin Genet Dev 21 113 119 21255998 10.1016/j.gde.2010.12.008 1:CAS:528:DC%2BC3MXhvFKjtLc%3D
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 113-119
    • Mathew, R.1    White, E.2
  • 10
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • DOI 10.1128/EC.01.1.11-21.2002
    • F Reggiori DJ Klionsky 2002 Autophagy in the eukaryotic cell Eukaryotic Cell 1 11 21 12455967 10.1128/EC.01.1.11-21.2002 1:CAS:528:DC%2BD38XitVSls74%3D (Pubitemid 36562345)
    • (2002) Eukaryotic Cell , vol.1 , Issue.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 11
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • 20855505 10.1083/jcb.200912089 1:CAS:528:DC%2BC3cXht1ahsbjJ
    • M Mari J Griffith E Rieter L Krishnappa DJ Klionsky F Reggiori 2010 An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis J Cell Biol 190 1005 1022 20855505 10.1083/jcb.200912089 1:CAS:528:DC%2BC3cXht1ahsbjJ
    • (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
  • 12
    • 77950462712 scopus 로고    scopus 로고
    • Where do they come from? Insights into autophagosome formation
    • 20188731 10.1016/j.febslet.2010.02.061 1:CAS:528:DC%2BC3cXjs12nu78%3D
    • M Hamasaki T Yoshimori 2010 Where do they come from? Insights into autophagosome formation FEBS Lett 584 1296 1301 20188731 10.1016/j.febslet.2010. 02.061 1:CAS:528:DC%2BC3cXjs12nu78%3D
    • (2010) FEBS Lett , vol.584 , pp. 1296-1301
    • Hamasaki, M.1    Yoshimori, T.2
  • 13
    • 77956414236 scopus 로고    scopus 로고
    • The origin of the autophagosomal membrane
    • 20811355 10.1038/ncb0910-831 1:CAS:528:DC%2BC3cXhtFSju7zK
    • SA Tooze T Yoshimori 2010 The origin of the autophagosomal membrane Nat Cell Biol 12 831 835 20811355 10.1038/ncb0910-831 1:CAS:528:DC%2BC3cXhtFSju7zK
    • (2010) Nat Cell Biol , vol.12 , pp. 831-835
    • Tooze, S.A.1    Yoshimori, T.2
  • 14
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • 18725538 10.1083/jcb.200803137 1:CAS:528:DC%2BD1cXhtV2rurzK
    • EL Axe SA Walker M Manifava P Chandra HL Roderick A Habermann G Griffiths NT Ktistakis 2008 Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum J Cell Biol 182 685 701 18725538 10.1083/jcb.200803137 1:CAS:528:DC%2BD1cXhtV2rurzK
    • (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
  • 15
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • 19898463 10.1038/ncb1991 1:CAS:528:DC%2BD1MXhsV2gsLnE
    • M Hayashi-Nishino N Fujita T Noda A Yamaguchi T Yoshimori A Yamamoto 2009 A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation Nat Cell Biol 11 1433 1437 19898463 10.1038/ncb1991 1:CAS:528:DC%2BD1MXhsV2gsLnE
    • (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
  • 16
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • 19855179 10.4161/auto.5.8.10274
    • P Ylä-Anttila H Vihinen E Jokitalo EL Eskelinen 2009 3D tomography reveals connections between the phagophore and endoplasmic reticulum Autophagy 5 1180 1185 19855179 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
  • 17
    • 77952495224 scopus 로고    scopus 로고
    • Mitochondria supply membranes for autophagosome biogenesis during starvation
    • 20478256 10.1016/j.cell.2010.04.009 1:CAS:528:DC%2BC3cXms1egsr8%3D
    • DW Hailey AS Rambold P Satpute-Krishnan K Mitra R Sougrat PK Kim J Lippincott-Schwartz 2010 Mitochondria supply membranes for autophagosome biogenesis during starvation Cell 141 656 667 20478256 10.1016/j.cell.2010.04. 009 1:CAS:528:DC%2BC3cXms1egsr8%3D
    • (2010) Cell , vol.141 , 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    Lippincott-Schwartz, J.7
  • 18
    • 67549139908 scopus 로고    scopus 로고
    • Vesicular trafficking and autophagosome formation
    • 19373247 10.1038/cdd.2009.39 1:CAS:528:DC%2BD1MXnsV2qs7w%3D
    • A Longatti SA Tooze 2009 Vesicular trafficking and autophagosome formation Cell Death Differ 16 956 965 19373247 10.1038/cdd.2009.39 1:CAS:528:DC%2BD1MXnsV2qs7w%3D
    • (2009) Cell Death Differ , vol.16 , pp. 956-965
    • Longatti, A.1    Tooze, S.A.2
  • 19
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: How does the end begin?
    • 19424283 10.1038/cdd.2009.54 1:CAS:528:DC%2BD1MXnsV2qsrY%3D
    • T Noda N Fujita T Yoshimori 2009 The late stages of autophagy: how does the end begin? Cell Death Differ 16 984 990 19424283 10.1038/cdd.2009.54 1:CAS:528:DC%2BD1MXnsV2qsrY%3D
    • (2009) Cell Death Differ , vol.16 , pp. 984-990
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 20
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • 20639694 10.4161/auto.6.6.12709 1:CAS:528:DC%2BC3cXhtFCqsrrP
    • E Itakura N Mizushima 2010 Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins Autophagy 6 764 776 20639694 10.4161/auto.6.6.12709 1:CAS:528:DC%2BC3cXhtFCqsrrP
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 21
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • 20034776 10.1016/j.ceb.2009.11.014 1:CAS:528:DC%2BC3cXks1SrtL4%3D
    • Z Yang DJ Klionsky 2010 Mammalian autophagy: core molecular machinery and signaling regulation Curr Opin Cell Biol 22 124 131 20034776 10.1016/j.ceb.2009.11.014 1:CAS:528:DC%2BC3cXks1SrtL4%3D
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 22
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • 21258367 10.1038/ncb2152 1:CAS:528:DC%2BC3MXhtlamtb0%3D
    • J Kim M Kundu B Viollet KL Guan 2011 AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1 Nat Cell Biol 13 132 141 21258367 10.1038/ncb2152 1:CAS:528:DC%2BC3MXhtlamtb0%3D
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 23
    • 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, PII S1534580703004027
    • F Reggiori KA Tucker PE Stromhaug DJ Klionsky 2004 The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure Dev Cell 6 79 90 14723849 10.1016/S1534-5807(03)00402-7 1:CAS:528:DC%2BD2cXntlaksQ%3D%3D (Pubitemid 38089207)
    • (2004) Developmental Cell , vol.6 , Issue.1 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 25
    • 39449108917 scopus 로고    scopus 로고
    • The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E07-08-0826
    • H Cheong U Nair J Geng DJ Klionsky 2008 The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae Mol Biol Cell 19 668 681 18077553 10.1091/mbc.E07-08-0826 1:CAS:528:DC%2BD1cXlslenur8%3D (Pubitemid 351272154)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 668-681
    • Cheong, H.1    Nair, U.2    Geng, J.3    Klionsky, D.J.4
  • 26
    • 65449186232 scopus 로고    scopus 로고
    • Atg17 recruits Atg9 to organize the pre-autophagosomal structure
    • 10.1111/j.1365-2443.2009.01299.x 1:CAS:528:DC%2BD1MXlvVCmurs%3D
    • T Sekito T Kawamata R Ichikawa K Suzuki Y Ohsumi 2009 Atg17 recruits Atg9 to organize the pre-autophagosomal structure Genes Cells Devot Mol Cell Mech 14 525 538 10.1111/j.1365-2443.2009.01299.x 1:CAS:528:DC%2BD1MXlvVCmurs%3D
    • (2009) Genes Cells Devot Mol Cell Mech , vol.14 , pp. 525-538
    • Sekito, T.1    Kawamata, T.2    Ichikawa, R.3    Suzuki, K.4    Ohsumi, Y.5
  • 27
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
    • 19797076 10.1083/jcb.200907014 1:CAS:528:DC%2BD1MXht1Srt7bO
    • A Simonsen SA Tooze 2009 Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes J Cell Biol 186 773 782 19797076 10.1083/jcb.200907014 1:CAS:528:DC%2BD1MXht1Srt7bO
    • (2009) J Cell Biol , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.A.2
  • 28
    • 77954197767 scopus 로고    scopus 로고
    • Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae
    • 20444982 10.1091/mbc.E09-04-0345
    • A van der Vaart J Griffith F Reggiori 2010 Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae Mol Biol Cell 21 2270 2284 20444982 10.1091/mbc.E09-04-0345
    • (2010) Mol Biol Cell , vol.21 , pp. 2270-2284
    • Van Der Vaart, A.1    Griffith, J.2    Reggiori, F.3
  • 29
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • 18321988 10.1091/mbc.E07-12-1257 1:CAS:528:DC%2BD1cXlslelsL0%3D
    • N Fujita T Itoh H Omori M Fukuda T Noda T Yoshimori 2008 The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy Mol Biol Cell 19 2092 2100 18321988 10.1091/mbc.E07-12-1257 1:CAS:528:DC%2BD1cXlslelsL0%3D
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 31
    • 67549096696 scopus 로고    scopus 로고
    • Bif-1/endophilin B1: A candidate for crescent driving force in autophagy
    • 19265852 10.1038/cdd.2009.19 1:CAS:528:DC%2BD1MXnsV2qs7c%3D
    • Y Takahashi CL Meyerkord HG Wang 2009 Bif-1/endophilin B1: a candidate for crescent driving force in autophagy Cell Death Differ 16 947 955 19265852 10.1038/cdd.2009.19 1:CAS:528:DC%2BD1MXnsV2qs7c%3D
    • (2009) Cell Death Differ , vol.16 , pp. 947-955
    • Takahashi, Y.1    Meyerkord, C.L.2    Wang, H.G.3
  • 32
    • 77951234553 scopus 로고    scopus 로고
    • Membrane trafficking events that partake in autophagy
    • 20036114 10.1016/j.ceb.2009.11.013 1:CAS:528:DC%2BC3cXks1SrtLs%3D
    • A Orsi HEJ Polson SA Tooze 2010 Membrane trafficking events that partake in autophagy Curr Opin Cell Biol 22 150 156 20036114 10.1016/j.ceb.2009.11.013 1:CAS:528:DC%2BC3cXks1SrtLs%3D
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 150-156
    • Orsi, A.1    Polson, H.E.J.2    Tooze, S.A.3
  • 33
    • 78649751019 scopus 로고    scopus 로고
    • The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
    • 21118109 10.1042/BST0381469 1:CAS:528:DC%2BC3cXhsFSkurrM
    • D Metcalf AM Isaacs 2010 The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes Biochem Soc Trans 38 1469 1473 21118109 10.1042/BST0381469 1:CAS:528:DC%2BC3cXhsFSkurrM
    • (2010) Biochem Soc Trans , vol.38 , pp. 1469-1473
    • Metcalf, D.1    Isaacs, A.M.2
  • 34
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • 19364919 10.1083/jcb.200810098 1:CAS:528:DC%2BD1MXlt1yjtLw%3D
    • M Razi EYW Chan SA Tooze 2009 Early endosomes and endosomal coatomer are required for autophagy J Cell Biol 185 305 321 19364919 10.1083/jcb.200810098 1:CAS:528:DC%2BD1MXlt1yjtLw%3D
    • (2009) J Cell Biol , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.W.2    Tooze, S.A.3
  • 35
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: Two closely related partners
    • 19008921 10.1038/cdd.2008.168 1:CAS:528:DC%2BD1cXhsV2it7%2FO
    • CM Fader MI Colombo 2009 Autophagy and multivesicular bodies: two closely related partners Cell Death Differ 16 70 78 19008921 10.1038/cdd.2008.168 1:CAS:528:DC%2BD1cXhsV2it7%2FO
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 37
    • 77955239270 scopus 로고    scopus 로고
    • Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites
    • 20545908 10.1111/j.1600-0854.2010.01086.x 1:CAS:528:DC%2BC3cXhtFSltLrL
    • FCM Zoppino RD Militello I Slavin C Alvarez MI Colombo 2010 Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites Traffic 11 1246 1261 20545908 10.1111/j.1600-0854.2010.01086.x 1:CAS:528: DC%2BC3cXhtFSltLrL
    • (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
  • 38
    • 77953801358 scopus 로고    scopus 로고
    • Regulation of mTORC1 by the Rab and Arf GTPases
    • 20457610 10.1074/jbc.C110.102483 1:CAS:528:DC%2BC3cXnsFygsr0%3D
    • L Li E Kim H Yuan K Inoki P Goraksha-Hicks RL Schiesher TP Neufeld KL Guan 2010 Regulation of mTORC1 by the Rab and Arf GTPases J Biol Chem 285 19705 19709 20457610 10.1074/jbc.C110.102483 1:CAS:528:DC%2BC3cXnsFygsr0%3D
    • (2010) J Biol Chem , vol.285 , pp. 19705-19709
    • Li, L.1    Kim, E.2    Yuan, H.3    Inoki, K.4    Goraksha-Hicks, P.5    Schiesher, R.L.6    Neufeld, T.P.7    Guan, K.L.8
  • 39
    • 0036017758 scopus 로고    scopus 로고
    • Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24
    • DOI 10.1034/j.1600-0854.2002.30704.x
    • DB Munafó MI Colombo 2002 Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24 Traffic 3 472 482 12047555 10.1034/j.1600-0854.2002.30704.x (Pubitemid 34692977)
    • (2002) Traffic , vol.3 , Issue.7 , pp. 472-482
    • Munafo, D.B.1    Colombo, M.I.2
  • 40
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • 18448665 10.1091/mbc.E07-12-1231 1:CAS:528:DC%2BD1cXoslWitL0%3D
    • T Itoh N Fujita E Kanno A Yamamoto T Yoshimori M Fukuda 2008 Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation Mol Biol Cell 19 2916 2925 18448665 10.1091/mbc.E07-12- 1231 1:CAS:528:DC%2BD1cXoslWitL0%3D
    • (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
  • 41
    • 79551546749 scopus 로고    scopus 로고
    • Autophagic substrate clearance requires activity of the syntaxin-5 SNARE complex
    • 21242315 10.1242/jcs.076489 1:CAS:528:DC%2BC3MXisFyjsrg%3D
    • M Renna C Schaffner AR Winslow FM Menzies AA Peden RA Floto DC Rubinsztein 2011 Autophagic substrate clearance requires activity of the syntaxin-5 SNARE complex J Cell Sci 124 469 482 21242315 10.1242/jcs.076489 1:CAS:528:DC%2BC3MXisFyjsrg%3D
    • (2011) J Cell Sci , vol.124 , pp. 469-482
    • Renna, M.1    Schaffner, C.2    Winslow, A.R.3    Menzies, F.M.4    Peden, A.A.5    Floto, R.A.6    Rubinsztein, D.C.7
  • 42
    • 46249127490 scopus 로고    scopus 로고
    • Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease
    • DOI 10.1242/jcs.025726
    • B Ravikumar S Imarisio S Sarkar CJ O'Kane DC Rubinsztein 2008 Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease J Cell Sci 121 1649 1660 18430781 10.1242/jcs.025726 1:CAS:528:DC%2BD1cXotVyiurs%3D (Pubitemid 351911822)
    • (2008) Journal of Cell Science , vol.121 , Issue.10 , pp. 1649-1660
    • Ravikumar, B.1    Imarisio, S.2    Sarkar, S.3    O'Kane, C.J.4    Rubinsztein, D.C.5
  • 43
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • DOI 10.1242/jcs.01114
    • MG Gutierrez DB Munafó W Berón MI Colombo 2004 Rab7 is required for the normal progression of the autophagic pathway in mammalian cells J Cell Sci 117 2687 2697 15138286 10.1242/jcs.01114 1:CAS:528: DC%2BD2cXlvFeht74%3D (Pubitemid 38997252)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafo, D.B.2    Beron, W.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
    • 19781582 10.1016/j.bbamcr.2009.09.011 1:CAS:528:DC%2BD1MXhsV2gsbzE
    • CM Fader DG Sánchez MB Mestre MI Colombo 2009 TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways Biochim Biophys Acta 1793 1901 1916 19781582 10.1016/j.bbamcr.2009.09.011 1:CAS:528:DC%2BD1MXhsV2gsbzE
    • (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
  • 46
    • 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
    • 20089838 10.1091/mbc.E09-08-0693 1:CAS:528:DC%2BC3cXjs1eqsLo%3D
    • N Furuta N Fujita T Noda T Yoshimori A Amano 2010 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 21 1001 1010 20089838 10.1091/mbc.E09-08-0693 1:CAS:528:DC%2BC3cXjs1eqsLo%3D
    • (2010) Mol Biol Cell , vol.21 , pp. 1001-1010
    • Furuta, N.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4    Amano, A.5
  • 47
    • 77957234857 scopus 로고    scopus 로고
    • The Rab GTPase RabG3b functions in autophagy and contributes to tracheary element differentiation in Arabidopsis
    • 1:CAS:528:DC%2BC3cXhtlCqt7%2FL
    • SI Kwon HJ Cho JH Jung K Yoshimoto K Shirasu OK Park 2010 The Rab GTPase RabG3b functions in autophagy and contributes to tracheary element differentiation in Arabidopsis Plant J Cell Mol Biol 64 151 164 1:CAS:528:DC%2BC3cXhtlCqt7%2FL
    • (2010) Plant J Cell Mol Biol , vol.64 , pp. 151-164
    • Kwon, S.I.1    Cho, H.J.2    Jung, J.H.3    Yoshimoto, K.4    Shirasu, K.5    Park, O.K.6
  • 49
    • 0037175026 scopus 로고    scopus 로고
    • Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs
    • DOI 10.1074/jbc.M205783200
    • A De Antoni J Schmitzová HH Trepte D Gallwitz S Albert 2002 Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs J Biol Chem 277 41023 41031 12189143 10.1074/jbc.M205783200 (Pubitemid 35215692)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41023-41031
    • De Antoni, A.1    Schmitzova, J.2    Trepte, H.-H.3    Gallwitz, D.4    Albert, S.5
  • 51
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • 11102533 1:CAS:528:DC%2BD3cXovFantro%3D
    • S Jones C Newman F Liu N Segev 2000 The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32 Mol Biol Cell 11 4403 4411 11102533 1:CAS:528:DC%2BD3cXovFantro%3D
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 52
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • 11038176 10.1083/jcb.151.2.289 1:CAS:528:DC%2BD3cXnsVaqsL8%3D
    • W Wang M Sacher S Ferro-Novick 2000 TRAPP stimulates guanine nucleotide exchange on Ypt1p J Cell Biol 151 289 296 11038176 10.1083/jcb.151.2.289 1:CAS:528:DC%2BD3cXnsVaqsL8%3D
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 53
    • 77958487311 scopus 로고    scopus 로고
    • TRAPP complexes in membrane traffic: Convergence through a common Rab. Nature reviews
    • 1:CAS:528:DC%2BC3cXhtlWmu7bO
    • J Barrowman D Bhandari K Reinisch S Ferro-Novick 2010 TRAPP complexes in membrane traffic: convergence through a common Rab. Nature reviews Mol Cell Biol 11 759 763 1:CAS:528:DC%2BC3cXhtlWmu7bO
    • (2010) Mol Cell Biol , vol.11 , pp. 759-763
    • Barrowman, J.1    Bhandari, D.2    Reinisch, K.3    Ferro-Novick, S.4
  • 54
    • 0035102194 scopus 로고    scopus 로고
    • TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport
    • DOI 10.1016/S1097-2765(01)00190-3
    • M Sacher J Barrowman W Wang J Horecka Y Zhang M Pypaert S Ferro-Novick 2001 TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport Mol Cell 7 433 442 11239471 10.1016/S1097-2765(01)00190-3 1:CAS:528: DC%2BD3MXis1KitLo%3D (Pubitemid 32206510)
    • (2001) Molecular Cell , vol.7 , Issue.2 , pp. 433-442
    • Sacher, M.1    Barrowman, J.2    Wang, W.3    Horecka, J.4    Zhang, Y.5    Pypaert, M.6    Ferro-Novick, S.7
  • 55
    • 70350115572 scopus 로고    scopus 로고
    • MTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles
    • 19656848 10.1091/mbc.E09-05-0387 1:CAS:528:DC%2BD1MXhsVSltLnI
    • A Yamasaki S Menon S Yu J Barrowman T Meerloo V Oorschot J Klumperman A Satoh S Ferro-Novick 2009 mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles Mol Biol Cell 20 4205 4215 19656848 10.1091/mbc.E09-05-0387 1:CAS:528:DC%2BD1MXhsVSltLnI
    • (2009) Mol Biol Cell , vol.20 , pp. 4205-4215
    • Yamasaki, A.1    Menon, S.2    Yu, S.3    Barrowman, J.4    Meerloo, T.5    Oorschot, V.6    Klumperman, J.7    Satoh, A.8    Ferro-Novick, S.9
  • 56
    • 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
    • DOI 10.1074/jbc.M501701200
    • K Meiling-Wesse UD Epple R Krick H Barth A Appelles C Voss EL Eskelinen M Thumm 2005 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 280 33669 33678 16079147 10.1074/jbc.M501701200 1:CAS:528:DC%2BD2MXhtVensbzJ (Pubitemid 41397169)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , 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    Tnumm, M.8
  • 57
    • 33845345128 scopus 로고    scopus 로고
    • Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae
    • 16874038 10.4161/auto.1.1.1512 1:CAS:528:DC%2BD2MXos1ensLk%3D
    • TY Nazarko J Huang JM Nicaud DJ Klionsky AA Sibirny 2005 Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae Autophagy 1 37 45 16874038 10.4161/auto.1.1.1512 1:CAS:528:DC%2BD2MXos1ensLk%3D
    • (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
  • 58
    • 0031976094 scopus 로고    scopus 로고
    • Getting into the Golgi
    • DOI 10.1016/S0962-8924(97)01184-7, PII S0962892497011847
    • SI Bannykh N Nishimura WE Balch 1998 Getting into the Golgi Trends Cell Biol 8 21 25 9695803 10.1016/S0962-8924(97)01184-7 1:CAS:528: DyaK1cXpt1WqtQ%3D%3D (Pubitemid 28040842)
    • (1998) Trends in Cell Biology , vol.8 , Issue.1 , pp. 21-25
    • Bannykh, S.I.1    Nishimura, N.2    Balch, W.E.3
  • 59
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • 20562859 10.1038/nature09204 1:CAS:528:DC%2BC3cXns1Gis7Y%3D
    • C Behrends ME Sowa SP Gygi JW Harper 2010 Network organization of the human autophagy system Nature 466 68 76 20562859 10.1038/nature09204 1:CAS:528:DC%2BC3cXns1Gis7Y%3D
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 62
    • 0029910357 scopus 로고    scopus 로고
    • Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans
    • DOI 10.1074/jbc.271.47.30158
    • M Jin L Saucan MG Farquhar GE Palade 1996 Rab1a and multiple other Rab proteins are associated with the transcytotic pathway in rat liver J Biol Chem 271 30105 30113 8939959 10.1074/jbc.271.47.30158 1:CAS:528:DyaK28XntFOht7s%3D (Pubitemid 26389658)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 30158-30166
    • Linder, B.1    Jin, Z.2    Freedman, J.H.3    Rubin, C.S.4
  • 63
    • 79952794950 scopus 로고    scopus 로고
    • Proteomic analysis of endocytic vesicles: Rab1a regulates motility of early endocytic vesicles
    • 21303926 10.1242/jcs.079020 1:CAS:528:DC%2BC3MXktVOru70%3D
    • A Mukhopadhyay E Nieves FY Che J Wang L Jin JW Murray K Gordon RH Angeletti AW Wolkoff 2011 Proteomic analysis of endocytic vesicles: Rab1a regulates motility of early endocytic vesicles J Cell Sci 124 765 775 21303926 10.1242/jcs.079020 1:CAS:528:DC%2BC3MXktVOru70%3D
    • (2011) J Cell Sci , vol.124 , pp. 765-775
    • Mukhopadhyay, A.1    Nieves, E.2    Che, F.Y.3    Wang, J.4    Jin, L.5    Murray, J.W.6    Gordon, K.7    Angeletti, R.H.8    Wolkoff, A.W.9
  • 64
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • DOI 10.1083/jcb.200109030
    • P Barbero L Bittova SR Pfeffer 2002 Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells J Cell Biol 156 511 518 11827983 10.1083/jcb.200109030 1:CAS:528:DC%2BD38XhtVOqtL8%3D (Pubitemid 34839898)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 65
    • 27144539169 scopus 로고    scopus 로고
    • Induced expressions of Rab24 GTPase and LC3 in nerve-injured motor neurons
    • DOI 10.1016/j.bbrc.2005.09.171, PII S0006291X05021650
    • Y Egami S Kiryu-Seo T Yoshimori H Kiyama 2005 Induced expressions of Rab24 GTPase and LC3 in nerve-injured motor neurons Biochem Biophys Res Commun 337 1206 1213 16236257 10.1016/j.bbrc.2005.09.171 1:CAS:528:DC%2BD2MXhtFKhs7fM (Pubitemid 41505252)
    • (2005) Biochemical and Biophysical Research Communications , vol.337 , Issue.4 , pp. 1206-1213
    • Egami, Y.1    Kiryu-Seo, S.2    Yoshimori, T.3    Kiyama, H.4
  • 67
    • 0031960166 scopus 로고    scopus 로고
    • A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae
    • JY Zheng T Koda T Fujiwara M Kishi Y Ikehara M Kakinuma 1998 A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae J Cell Sci 111 Pt 8 1061 1069 9512502 1:CAS:528:DyaK1cXjt1Khsr8%3D (Pubitemid 28227106)
    • (1998) Journal of Cell Science , vol.111 , Issue.8 , pp. 1061-1069
    • Zheng, J.Y.1    Koda, T.2    Fujiwara, T.3    Kishi, M.4    Ikehara, Y.5    Kakinuma, M.6
  • 68
    • 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
    • DOI 10.1016/S0014-5793(01)02993-3, PII S0014579301029933
    • R Valsdottir H Hashimoto K Ashman T Koda B Storrie T Nilsson 2001 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 508 201 209 11718716 10.1016/S0014-5793(01)02993-3 1:CAS:528:DC%2BD3MXosFKqtrw%3D (Pubitemid 33079246)
    • (2001) FEBS Letters , vol.508 , Issue.2 , pp. 201-209
    • Valsdottir, R.1    Hashimoto, H.2    Ashman, K.3    Koda, T.4    Storrie, B.5    Nilsson, T.6
  • 69
    • 77953144320 scopus 로고    scopus 로고
    • Rab33b and Rab6 are functionally overlapping regulators of Golgi homeostasis and trafficking
    • 20163571 10.1111/j.1600-0854.2010.01051.x 1:CAS:528:DC%2BC3cXlt1Kis7o%3D
    • T Starr Y Sun N Wilkins B Storrie 2010 Rab33b and Rab6 are functionally overlapping regulators of Golgi homeostasis and trafficking Traffic 11 626 636 20163571 10.1111/j.1600-0854.2010.01051.x 1:CAS:528:DC%2BC3cXlt1Kis7o%3D
    • (2010) Traffic , vol.11 , pp. 626-636
    • Starr, T.1    Sun, Y.2    Wilkins, N.3    Storrie, B.4
  • 70
    • 50249131810 scopus 로고    scopus 로고
    • Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals
    • 18670194 1:CAS:528:DC%2BD1cXhtVynt7bK
    • M Fukuda T Itoh 2008 Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals Autophagy 4 824 826 18670194 1:CAS:528:DC%2BD1cXhtVynt7bK
    • (2008) Autophagy , vol.4 , pp. 824-826
    • Fukuda, M.1    Itoh, T.2
  • 71
    • 24644440921 scopus 로고    scopus 로고
    • Exosome secretion and red cell maturation: Exploring molecular components involved in the docking and fusion of multivesicular bodies in K562 cells
    • DOI 10.1016/j.bcmd.2005.07.002, PII S1079979605001087
    • CM Fader A Savina D Sánchez MI Colombo 2005 Exosome secretion and red cell maturation: Exploring molecular components involved in the docking and fusion of multivesicular bodies in K562 cells Blood Cells Mol Dis 35 153 157 16099697 10.1016/j.bcmd.2005.07.002 1:CAS:528:DC%2BD2MXhtVSmurbM (Pubitemid 41267043)
    • (2005) Blood Cells, Molecules, and Diseases , vol.35 , Issue.2 , pp. 153-157
    • Fader, C.M.1    Savina, A.2    Sanchez, D.3    Colombo, M.I.4
  • 72
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • 17999726 10.1111/j.1600-0854.2007.00677.x 1:CAS:528:DC%2BD1cXit1SgsbY%3D
    • CM Fader D Sánchez M Furlán MI Colombo 2008 Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells Traffic 9 230 250 17999726 10.1111/j.1600-0854.2007.00677.x 1:CAS:528:DC%2BD1cXit1SgsbY%3D
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.M.1    Sánchez, D.2    Furlán, M.3    Colombo, M.I.4
  • 73
    • 73549102459 scopus 로고    scopus 로고
    • An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7
    • 19956673 10.1371/journal.ppat.1000670
    • H Yamaguchi I Nakagawa A Yamamoto A Amano T Noda T Yoshimori 2009 An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7 PLoS pathogens 5 e1000670 19956673 10.1371/journal.ppat.1000670
    • (2009) PLoS Pathogens , vol.5 , pp. 1000670
    • Yamaguchi, H.1    Nakagawa, I.2    Yamamoto, A.3    Amano, A.4    Noda, T.5    Yoshimori, T.6
  • 74
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • 20100911 10.1083/jcb.200907015 1:CAS:528:DC%2BC3cXhsVyjsL0%3D
    • S Pankiv EA Alemu A Brech JA Bruun T Lamark A Overvatn G Bjørkøy T Johansen 2010 FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport J Cell Biol 188 253 269 20100911 10.1083/jcb.200907015 1:CAS:528:DC%2BC3cXhsVyjsL0%3D
    • (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
  • 75
    • 38849147752 scopus 로고    scopus 로고
    • Ral GTPases and cancer: Linchpin support of the tumorigenic platform
    • DOI 10.1038/nrc2296, PII NRC2296
    • BO Bodemann MA White 2008 Ral GTPases and cancer: linchpin support of the tumorigenic platform. Nature reviews Cancer 8 133 140 18219307 1:CAS:528:DC%2BD1cXhtVGhs78%3D (Pubitemid 351187648)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.2 , pp. 133-140
    • Bodemann, B.O.1    White, M.A.2
  • 76
    • 20444393402 scopus 로고    scopus 로고
    • Ral GTPases: Corrupting the exocyst in cancer cells
    • DOI 10.1016/j.tcb.2005.04.002, PII S0962892405001017
    • JH Camonis MA White 2005 Ral GTPases: corrupting the exocyst in cancer cells Trends Cell Biol 15 327 332 15953551 10.1016/j.tcb.2005.04.002 1:CAS:528:DC%2BD2MXlt1Srt74%3D (Pubitemid 40805329)
    • (2005) Trends in Cell Biology , vol.15 , Issue.6 , pp. 327-332
    • Camonis, J.H.1    White, M.A.2
  • 77
    • 67949106616 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • 19473826 10.1016/j.ceb.2009.04.007 1:CAS:528:DC%2BD1MXps1Cltbo%3D
    • B He W Guo 2009 The exocyst complex in polarized exocytosis Curr Opin Cell Biol 21 537 542 19473826 10.1016/j.ceb.2009.04.007 1:CAS:528: DC%2BD1MXps1Cltbo%3D
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 537-542
    • He, B.1    Guo, W.2
  • 80
    • 0036608158 scopus 로고    scopus 로고
    • Ras family therapy: Rab, Rho and Ral talk to the exocyst
    • DOI 10.1016/S0962-8924(02)02293-6, PII S0962892402022936
    • P Novick W Guo 2002 Ras family therapy: Rab, Rho and Ral talk to the exocyst Trends Cell Biol 12 247 249 12074877 10.1016/S0962-8924(02)02293-6 1:CAS:528:DC%2BD38Xks1emurw%3D (Pubitemid 34634167)
    • (2002) Trends in Cell Biology , vol.12 , Issue.6 , pp. 247-249
    • Novick, P.1    Guo, W.2
  • 81
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: Membrane interactions and toxicity in Parkinson's disease
    • 20500090 10.1146/annurev.cellbio.042308.113313 1:CAS:528: DC%2BC3cXhsFCnur7F
    • PK Auluck G Caraveo S Lindquist 2010 α-Synuclein: membrane interactions and toxicity in Parkinson's disease Annu Rev Cell Dev Biol 26 211 233 20500090 10.1146/annurev.cellbio.042308.113313 1:CAS:528:DC%2BC3cXhsFCnur7F
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 82
    • 79957963356 scopus 로고    scopus 로고
    • Rabs, SNAREs and α-synuclein-membrane trafficking defects in synucleinopathies
    • Chua CEL, Tang BL (2011) Rabs, SNAREs and α-synuclein-membrane trafficking defects in synucleinopathies. Brain Res Rev
    • (2011) Brain Res Rev
    • Cel, C.1    Tang, B.L.2
  • 83
    • 55949092886 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and neurodegenerative diseases
    • 18855701 10.2174/138920308785915218 1:CAS:528:DC%2BD1cXhtFKnur3I
    • VN Uversky 2008 Alpha-synuclein misfolding and neurodegenerative diseases Curr Protein Pept Sci 9 507 540 18855701 10.2174/138920308785915218 1:CAS:528:DC%2BD1cXhtFKnur3I
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 507-540
    • Uversky, V.N.1
  • 87
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • DOI 10.1126/science.290.5500.2298
    • S Naureckiene DE Sleat H Lackland A Fensom MT Vanier R Wattiaux M Jadot P Lobel 2000 Identification of HE1 as the second gene of Niemann-Pick C disease Science 290 2298 2301 11125141 10.1126/science.290.5500.2298 1:CAS:528:DC%2BD3cXptFSmsro%3D (Pubitemid 32041569)
    • (2000) Science , vol.290 , Issue.5500 , pp. 2298-2301
    • Naureckiene, S.1    Sleat, D.E.2    Lacklan, H.3    Fensom, A.4    Vanier, M.T.5    Wattiaux, R.6    Jadot, M.7    Lobel, P.8
  • 88
    • 36148991943 scopus 로고    scopus 로고
    • Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease
    • 16103921 10.1371/journal.pgen.0010081 1:CAS:528:DC%2BD2MXmvVekt7g%3D
    • DC Ko L Milenkovic SM Beier H Manuel J Buchanan MP Scott 2005 Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease PLoS Genet 1 81 95 16103921 10.1371/journal.pgen. 0010081 1:CAS:528:DC%2BD2MXmvVekt7g%3D
    • (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
  • 89
    • 24644494640 scopus 로고    scopus 로고
    • Protein transduction of Rab9 in Niemann-Pick C cells reduces cholesterol storage
    • DOI 10.1096/fj.04-2714fje
    • K Narita A Choudhury K Dobrenis DK Sharma EL Holicky DL Marks SU Walkley RE Pagano 2005 Protein transduction of Rab9 in Niemann-Pick C cells reduces cholesterol storage FASEB J Off Publ Fed Am Soc Exp Biol 19 1558 1560 1:CAS:528:DC%2BD2MXpvF2gtb0%3D (Pubitemid 41279030)
    • (2005) FASEB Journal , vol.19 , Issue.11 , pp. 1558-1560
    • Narita, K.1    Choudhury, A.2    Dobrenis, K.3    Sharma, D.K.4    Holicky, E.L.5    Marks, D.L.6    Walkley, S.U.7    Pagano, R.E.8
  • 90
    • 33846089323 scopus 로고    scopus 로고
    • Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells
    • DOI 10.1091/mbc.E06-07-0575
    • MD Linder RL Uronen M Hölttä-Vuori P van der Sluijs J Peränen E Ikonen 2007 Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells Mol Biol Cell 18 47 56 17050734 10.1091/mbc.E06-07-0575 1:CAS:528:DC%2BD2sXmsFygtQ%3D%3D (Pubitemid 46066709)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.1 , pp. 47-56
    • Linder, M.D.1    Uronen, R.-L.2    Holtta-Vuori, M.3    Van Der Sluijs, P.4    Peranen, J.5    Ikonen, E.6
  • 91
    • 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
    • 19056848 10.2353/ajpath.2009.080660 1:CAS:528:DC%2BD1MXhslOlurg%3D
    • T Kaptzan SA West EL Holicky CL Wheatley DL Marks T Wang KB Peake J Vance SU Walkley RE Pagano 2009 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 174 14 20 19056848 10.2353/ajpath.2009.080660 1:CAS:528:DC%2BD1MXhslOlurg%3D
    • (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
  • 92
    • 23844472876 scopus 로고    scopus 로고
    • RalA and RalB: Antagonistic relatives in cancer cell migration
    • DOI 10.1158/0008-5472.CAN-04-1957
    • G Oxford CR Owens BJ Titus TL Foreman MC Herlevsen SC Smith D Theodorescu 2005 RalA and RalB: antagonistic relatives in cancer cell migration Cancer Res 65 7111 7120 16103060 10.1158/0008-5472.CAN-04-1957 1:CAS:528: DC%2BD2MXns1WrtLY%3D (Pubitemid 41161240)
    • (2005) Cancer Research , vol.65 , Issue.16 , pp. 7111-7120
    • Oxford, G.1    Owens, C.R.2    Titus, B.J.3    Foreman, T.L.4    Herlevsen, M.C.5    Smith, S.C.6    Theodorescu, D.7
  • 93
    • 58049216316 scopus 로고    scopus 로고
    • RalA functions as an indispensable signal mediator for the nutrient-sensing system
    • 18948269 10.1074/jbc.M805822200 1:CAS:528:DC%2BD1cXhsVGqt7%2FK
    • T Maehama M Tanaka H Nishina M Murakami Y Kanaho K Hanada 2008 RalA functions as an indispensable signal mediator for the nutrient-sensing system J Biol Chem 283 35053 35059 18948269 10.1074/jbc.M805822200 1:CAS:528: DC%2BD1cXhsVGqt7%2FK
    • (2008) J Biol Chem , vol.283 , pp. 35053-35059
    • Maehama, T.1    Tanaka, M.2    Nishina, H.3    Murakami, M.4    Kanaho, Y.5    Hanada, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.