메뉴 건너뛰기




Volumn 1298, Issue , 2015, Pages

Rab family of GTpases

(2)  Li, Guangpu a   Marlin, M Caleb a  

a NONE

Author keywords

Effector; GAP; GEF; GTP binding protein; GTPase; Membrane trafficking; Rab; Vesicular transport

Indexed keywords

GROWTH FACTOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; HORMONE; MEMBRANE RECEPTOR; RAB PROTEIN; SECRETORY PROTEIN;

EID: 84925935479     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2569-8_1     Document Type: Article
Times cited : (160)

References (112)
  • 1
    • 80055078598 scopus 로고    scopus 로고
    • Thousands of rab GTPases for the cell biologist
    • Diekmann Y, Seixas E, Gouw M et al (2011) Thousands of rab GTPases for the cell biologist. PLoS Comput Biol 7:e1002217
    • (2011) Plos Comput Biol , vol.7
    • Diekmann, Y.1    Seixas, E.2    Gouw, M.3
  • 2
    • 84865378898 scopus 로고    scopus 로고
    • Untangling the evolution of Rab G proteins: Implications of a comprehensive genomic analysis
    • Klopper TH, Kienle N, Fasshauer D et al (2012) Untangling the evolution of Rab G proteins: implications of a comprehensive genomic analysis. BMC Biol 10:71
    • (2012) BMC Biol , vol.10
    • Klopper, T.H.1    Kienle, N.2    Fasshauer, D.3
  • 3
    • 84882727744 scopus 로고    scopus 로고
    • Ypt/Rab GTPases and Intracellular Membrane Trafficking: An Overview
    • Li G, Segev N (eds), Bentham Science Publishers, Sharjah
    • Li G, Segev N (2012) Ypt/Rab GTPases and Intracellular Membrane Trafficking: an Overview. In: Li G, Segev N (eds) Rab GTPases and Membrane Trafficking. Bentham Science Publishers, Sharjah, pp 3-17
    • (2012) Rab Gtpases and Membrane Trafficking , pp. 3-17
    • Li, G.1    Segev, N.2
  • 5
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • Hutagalung AH, Novick PJ (2011) Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev 91:119-149
    • (2011) Physiol Rev , vol.91 , pp. 119-149
    • Hutagalung, A.H.1    Novick, P.J.2
  • 6
    • 84883454656 scopus 로고    scopus 로고
    • Rab GTPase regulation of membrane identity
    • Pfeffer SR (2013) Rab GTPase regulation of membrane identity. Curr Opin Cell Biol 25:414-419
    • (2013) Curr Opin Cell Biol , vol.25 , pp. 414-419
    • Pfeffer, S.R.1
  • 7
    • 0025363426 scopus 로고
    • Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
    • Chavrier P, Parton RG, Hauri HP et al (1990) Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62:317-329
    • (1990) Cell , vol.62 , pp. 317-329
    • Chavrier, P.1    Parton, R.G.2    Hauri, H.P.3
  • 8
    • 84874366009 scopus 로고    scopus 로고
    • RabGEFs are a major determinant for specific Rab membrane targeting
    • Blumer J, Rey J, Dehmelt L et al (2013) RabGEFs are a major determinant for specific Rab membrane targeting. J Cell Biol 200: 287-300
    • (2013) J Cell Biol , vol.200 , pp. 287-300
    • Blumer, J.1    Rey, J.2    Dehmelt, L.3
  • 9
    • 0242363237 scopus 로고    scopus 로고
    • Yip3 catalyses the dissociation of endosomal Rab-GDI complexes
    • Sivars U, Aivazian D, Pfeffer SR (2003) Yip3 catalyses the dissociation of endosomal Rab-GDI complexes. Nature 425:856-859
    • (2003) Nature , vol.425 , pp. 856-859
    • Sivars, U.1    Aivazian, D.2    Pfeffer, S.R.3
  • 10
    • 0028207180 scopus 로고
    • Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange
    • Soldati T, Shapiro AD, Svejstrup AB et al (1994) Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 369:76-78
    • (1994) Nature , vol.369 , pp. 76-78
    • Soldati, T.1    Shapiro, A.D.2    Svejstrup, A.B.3
  • 11
    • 0028326049 scopus 로고
    • Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange
    • Ullrich O, Horiuchi H, Bucci C et al (1994) Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange. Nature 368:157-160
    • (1994) Nature , vol.368 , pp. 157-160
    • Ullrich, O.1    Horiuchi, H.2    Bucci, C.3
  • 13
    • 0027418539 scopus 로고
    • Rab GDI: A solubilizing and recycling factor for rab9 protein
    • Soldati T, Riederer MA, Pfeffer SR (1993) Rab GDI: a solubilizing and recycling factor for rab9 protein. Mol Biol Cell 4:425-434
    • (1993) Mol Biol Cell , vol.4 , pp. 425-434
    • Soldati, T.1    Riederer, M.A.2    Pfeffer, S.R.3
  • 14
    • 0027525327 scopus 로고
    • Interaction of Sec4 with GDI proteins from bovine brain, Drosophila melanogaster and Saccharomyces cerevisiae. Conservation of GDI membrane dissociation activity
    • Garrett MD, Kabcenell AK, Zahner JE et al (1993) Interaction of Sec4 with GDI proteins from bovine brain, Drosophila melanogaster and Saccharomyces cerevisiae. Conservation of GDI membrane dissociation activity. FEBS Lett 331:233-238
    • (1993) FEBS Lett , vol.331 , pp. 233-238
    • Garrett, M.D.1    Kabcenell, A.K.2    Zahner, J.E.3
  • 15
    • 0027202199 scopus 로고
    • Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins
    • Ullrich O, Stenmark H, Alexandrov K et al (1993) Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. J Biol Chem 268: 18143-18150
    • (1993) J Biol Chem , vol.268 , pp. 18143-18150
    • Ullrich, O.1    Stenmark, H.2    Alexandrov, K.3
  • 16
    • 30444436194 scopus 로고    scopus 로고
    • Vps9 domain-containing proteins: Activators of Rab5 GTPases from yeast to neurons
    • Carney DS, Davies BA, Horazdovsky BF (2006) Vps9 domain-containing proteins: activators of Rab5 GTPases from yeast to neurons. Trends Cell Biol 16:27-35
    • (2006) Trends Cell Biol , vol.16 , pp. 27-35
    • Carney, D.S.1    Davies, B.A.2    Horazdovsky, B.F.3
  • 17
    • 77957231342 scopus 로고    scopus 로고
    • The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7
    • Nordmann M, Cabrera M, Perz A et al (2010) The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7. Curr Biol 20:1654-1659
    • (2010) Curr Biol , vol.20 , pp. 1654-1659
    • Nordmann, M.1    Cabrera, M.2    Perz, A.3
  • 18
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev D, Datta S, Ackema K et al (2010) Identification of the switch in early-to-late endosome transition. Cell 141:497-508
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3
  • 19
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • Jones S, Newman C, Liu F et al (2000) The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell 11: 4403-4411
    • (2000) Mol Biol Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3
  • 20
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • Wang W, Sacher M, Ferro-Novick S (2000) TRAPP stimulates guanine nucleotide exchange on Ypt1p. J Cell Biol 151:289-296
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 21
    • 0036732902 scopus 로고    scopus 로고
    • A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling andpolarized membrane transport
    • Hattula K, Furuhjelm J, Arffman A et al (2002) A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling andpolarized membrane transport. Mol Biol Cell 13:3268-3280
    • (2002) Mol Biol Cell , vol.13 , pp. 3268-3280
    • Hattula, K.1    Furuhjelm, J.2    Arffman, A.3
  • 22
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou S, Peak-Chew SY, Pelham HR (2000) Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J 19:4885-4894
    • (2000) EMBO J , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.3
  • 23
    • 79954614556 scopus 로고    scopus 로고
    • DENN domain proteins: Regulators of Rab GTPases
    • Marat AL, Dokainish H, McPherson PS (2011) DENN domain proteins: regulators of Rab GTPases. J Biol Chem 286:13791-13800
    • (2011) J Biol Chem , vol.286 , pp. 13791-13800
    • Marat, A.L.1    Dokainish, H.2    McPherson, P.S.3
  • 24
    • 33746356908 scopus 로고    scopus 로고
    • TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    • Pan X, Eathiraj S, Munson M et al (2006) TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 442:303-306
    • (2006) Nature , vol.442 , pp. 303-306
    • Pan, X.1    Eathiraj, S.2    Munson, M.3
  • 25
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz D, Medkova M, Walch-Solimena C et al (2002) Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J Cell Biol 157:1005-1015
    • (2002) J Cell Biol , vol.157 , pp. 1005-1015
    • Ortiz, D.1    Medkova, M.2    Walch-Solimena, C.3
  • 26
    • 77950877404 scopus 로고    scopus 로고
    • Coordination of Rab8 and Rab11 in primary ciliogenesis
    • Knodler A, Feng S, Zhang J et al (2010) Coordination of Rab8 and Rab11 in primary ciliogenesis. Proc Natl Acad Sci U S A 107: 6346-6351
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 6346-6351
    • Knodler, A.1    Feng, S.2    Zhang, J.3
  • 27
    • 84871282415 scopus 로고    scopus 로고
    • Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase
    • Pusapati GV, Luchetti G, Pfeffer SR (2012) Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase. J Biol Chem 287:42129-42137
    • (2012) J Biol Chem , vol.287 , pp. 42129-42137
    • Pusapati, G.V.1    Luchetti, G.2    Pfeffer, S.R.3
  • 28
    • 73949094671 scopus 로고    scopus 로고
    • Rabex-5 is a Rab22 effector and mediates a Rab22-Rab5 signaling cascade in endocytosis
    • Zhu H, Liang Z, Li G (2009) Rabex-5 is a Rab22 effector and mediates a Rab22-Rab5 signaling cascade in endocytosis. Mol Biol Cell 20:4720-4729
    • (2009) Mol Biol Cell , vol.20 , pp. 4720-4729
    • Zhu, H.1    Liang, Z.2    Li, G.3
  • 29
    • 84869491973 scopus 로고    scopus 로고
    • BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor
    • Gerondopoulos A, Langemeyer L, Liang JR et al (2012) BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor. Curr Biol 22: 2135-2139
    • (2012) Curr Biol , vol.22 , pp. 2135-2139
    • Gerondopoulos, A.1    Langemeyer, L.2    Liang, J.R.3
  • 30
    • 77951248675 scopus 로고    scopus 로고
    • Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9
    • Kloer DP, Rojas R, Ivan V et al (2010) Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9. J Biol Chem 285: 7794-7804
    • (2010) J Biol Chem , vol.285 , pp. 7794-7804
    • Kloer, D.P.1    Rojas, R.2    Ivan, V.3
  • 31
    • 70149084564 scopus 로고    scopus 로고
    • A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway
    • Rivera-Molina FE, Novick PJ (2009) A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway. Proc Natl Acad Sci U S A 106:14408-14413
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14408-14413
    • Rivera-Molina, F.E.1    Novick, P.J.2
  • 32
    • 84863312340 scopus 로고    scopus 로고
    • RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36
    • Nottingham RM, Pusapati GV, Ganley IG et al (2012) RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36. J Biol Chem 287:22740-22748
    • (2012) J Biol Chem , vol.287 , pp. 22740-22748
    • Nottingham, R.M.1    Pusapati, G.V.2    Ganley, I.G.3
  • 33
    • 80053000783 scopus 로고    scopus 로고
    • RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins
    • Nottingham RM, Ganley IG, Barr FA et al (2011) RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. J Biol Chem 286: 33213-33222
    • (2011) J Biol Chem , vol.286 , pp. 33213-33222
    • Nottingham, R.M.1    Ganley, I.G.2    Barr, F.A.3
  • 35
    • 2142815184 scopus 로고    scopus 로고
    • Sensitivity and specificity amplification in signal transduction
    • Li G, Qian H (2003) Sensitivity and specificity amplification in signal transduction. Cell Biochem Biophys 39:45-59
    • (2003) Cell Biochem Biophys , vol.39 , pp. 45-59
    • Li, G.1    Qian, H.2
  • 36
    • 84880816067 scopus 로고    scopus 로고
    • Review series: Rab GTPases and membrane identity: Causal or inconsequential?
    • Barr FA (2013) Review series: Rab GTPases and membrane identity: causal or inconsequential? J Cell Biol 202:191-199
    • (2013) J Cell Biol , vol.202 , pp. 191-199
    • Barr, F.A.1
  • 37
    • 77952943084 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p
    • Mizuno-Yamasaki E, Medkova M, Coleman J et al (2010) Phosphatidylinositol 4-phosphate controls both membrane recruitment and a regulatory switch of the Rab GEF Sec2p. Dev Cell 18:828-840
    • (2010) Dev Cell , vol.18 , pp. 828-840
    • Mizuno-Yamasaki, E.1    Medkova, M.2    Coleman, J.3
  • 38
    • 84890284248 scopus 로고    scopus 로고
    • Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners
    • Stalder D, Mizuno-Yamasaki E, Ghassemian M et al (2013) Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners. Proc Natl Acad Sci U S A 110:19995-20002
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 19995-20002
    • Stalder, D.1    Mizuno-Yamasaki, E.2    Ghassemian, M.3
  • 39
    • 33747447033 scopus 로고    scopus 로고
    • Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins
    • Pellinen T, Arjonen A, Vuoriluoto K et al (2006) Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins. J Cell Biol 173:767-780
    • (2006) J Cell Biol , vol.173 , pp. 767-780
    • Pellinen, T.1    Arjonen, A.2    Vuoriluoto, K.3
  • 40
    • 51449087302 scopus 로고    scopus 로고
    • Integrin trafficking regulated by Rab21 is necessary for cytokinesis
    • Pellinen T, Tuomi S, Arjonen A et al (2008) Integrin trafficking regulated by Rab21 is necessary for cytokinesis. Dev Cell 15:371-385
    • (2008) Dev Cell , vol.15 , pp. 371-385
    • Pellinen, T.1    Tuomi, S.2    Arjonen, A.3
  • 41
    • 0037016681 scopus 로고    scopus 로고
    • Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion
    • Seachrist JL, Laporte SA, Dale LB et al (2002) Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion. J Biol Chem 277:679-685
    • (2002) J Biol Chem , vol.277 , pp. 679-685
    • Seachrist, J.L.1    Laporte, S.A.2    Dale, L.B.3
  • 42
    • 0036480017 scopus 로고    scopus 로고
    • Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells
    • Van IJzendoorn SC, Tuvim MJ, Weimbs T et al (2002) Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells. Dev Cell 2:219-228
    • (2002) Dev Cell , vol.2 , pp. 219-228
    • Van Ijzendoorn, S.C.1    Tuvim, M.J.2    Weimbs, T.3
  • 43
    • 0031983836 scopus 로고    scopus 로고
    • A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits
    • McLauchlan H, Newell J, Morrice N et al (1998) A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits. Curr Biol 8:34-45
    • (1998) Curr Biol , vol.8 , pp. 34-45
    • McLauchlan, H.1    Newell, J.2    Morrice, N.3
  • 44
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • Carroll KS, Hanna J, Simon I et al (2001) Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 292:1373-1376
    • (2001) Science , vol.292 , pp. 1373-1376
    • Carroll, K.S.1    Hanna, J.2    Simon, I.3
  • 45
    • 84887069906 scopus 로고    scopus 로고
    • Identification and characterization of multiple novel Rab-myosin Va interactions
    • Lindsay AJ, Jollivet F, Horgan CP et al (2013) Identification and characterization of multiple novel Rab-myosin Va interactions. Mol Biol Cell 24:3420-3434
    • (2013) Mol Biol Cell , vol.24 , pp. 3420-3434
    • Lindsay, A.J.1    Jollivet, F.2    Horgan, C.P.3
  • 46
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan B, Bowser R, Novick P (1995) The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol 128:1055-1068
    • (1995) J Cell Biol , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 47
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • Fukuda M, Kuroda TS, Mikoshiba K (2002) Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J Biol Chem 277: 12432-12436
    • (2002) J Biol Chem , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 48
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for myosin Va
    • Wu X, Wang F, Rao K et al (2002) Rab27a is an essential component of melanosome receptor for myosin Va. Mol Biol Cell 13:1735-1749
    • (2002) Mol Biol Cell , vol.13 , pp. 1735-1749
    • Wu, X.1    Wang, F.2    Rao, K.3
  • 49
    • 0037108473 scopus 로고    scopus 로고
    • The Rab6 GTPase regulates recruitmentof the dynactin complex to Golgi membranes
    • Short B, Preisinger C, Schaletzky J et al (2002) The Rab6 GTPase regulates recruitmentof the dynactin complex to Golgi membranes. Curr Biol 12:1792-1795
    • (2002) Curr Biol , vol.12 , pp. 1792-1795
    • Short, B.1    Preisinger, C.2    Schaletzky, J.3
  • 50
    • 40049101577 scopus 로고    scopus 로고
    • Rab6 family proteins interact with the dynein light chain protein DYNLRB1
    • Wanschers B, van de Vorstenbosch R, Wijers M et al (2008) Rab6 family proteins interact with the dynein light chain protein DYNLRB1. Cell Motil Cytoskeleton 65:183-196
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 183-196
    • Wanschers, B.1    Van De Vorstenbosch, R.2    Wijers, M.3
  • 51
    • 0032559265 scopus 로고    scopus 로고
    • Interaction of a Golgi-associated kinesin-like protein with Rab6
    • Echard A, Jollivet F, Martinez O et al (1998) Interaction of a Golgi-associated kinesin-like protein with Rab6. Science 279:580-585
    • (1998) Science , vol.279 , pp. 580-585
    • Echard, A.1    Jollivet, F.2    Martinez, O.3
  • 52
    • 78651456909 scopus 로고    scopus 로고
    • KIF16B/Rab14 molecular motor complex is critical for early embryonic development by transporting FGF receptor
    • Ueno H, Huang X, Tanaka Y et al (2011) KIF16B/Rab14 molecular motor complex is critical for early embryonic development by transporting FGF receptor. Dev Cell 20:60-71
    • (2011) Dev Cell , vol.20 , pp. 60-71
    • Ueno, H.1    Huang, X.2    Tanaka, Y.3
  • 53
    • 77950188464 scopus 로고    scopus 로고
    • Rab11-FIP3 binds dynein light intermediate chain 2 and its overexpression fragments the Golgi complex
    • Horgan CP, Hanscom SR, Jolly RS et al (2010) Rab11-FIP3 binds dynein light intermediate chain 2 and its overexpression fragments the Golgi complex. Biochem Biophys Res Commun 394:387-392
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 387-392
    • Horgan, C.P.1    Hanscom, S.R.2    Jolly, R.S.3
  • 54
    • 73849085073 scopus 로고    scopus 로고
    • Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment
    • Horgan CP, Hanscom SR, Jolly RS et al (2010) Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment. J Cell Sci 123:181-191
    • (2010) J Cell Sci , vol.123 , pp. 181-191
    • Horgan, C.P.1    Hanscom, S.R.2    Jolly, R.S.3
  • 55
    • 59549101542 scopus 로고    scopus 로고
    • The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling
    • Schonteich E, Wilson GM, Burden J et al (2008) The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling. J Cell Sci 121:3824-3833
    • (2008) J Cell Sci , vol.121 , pp. 3824-3833
    • Schonteich, E.1    Wilson, G.M.2    Burden, J.3
  • 56
    • 45249108704 scopus 로고    scopus 로고
    • Mechanisms regulating targeting of recycling endosomes to the cleavage furrow during cytokinesis
    • Simon GC, Prekeris R (2008) Mechanisms regulating targeting of recycling endosomes to the cleavage furrow during cytokinesis. Biochem Soc Trans 36:391-394
    • (2008) Biochem Soc Trans , vol.36 , pp. 391-394
    • Simon, G.C.1    Prekeris, R.2
  • 57
    • 18844384403 scopus 로고    scopus 로고
    • Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B
    • Hoepfner S, Severin F, Cabezas A et al (2005) Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B. Cell 121:437-450
    • (2005) Cell , vol.121 , pp. 437-450
    • Hoepfner, S.1    Severin, F.2    Cabezas, A.3
  • 58
    • 84855457001 scopus 로고    scopus 로고
    • Intrinsic tethering activity of endosomal Rab proteins
    • Lo SY, Brett CL, Plemel RL et al (2012) Intrinsic tethering activity of endosomal Rab proteins. Nat Struct Mol Biol 19:40-47
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 40-47
    • Lo, S.Y.1    Brett, C.L.2    Plemel, R.L.3
  • 59
    • 67649470529 scopus 로고    scopus 로고
    • Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes
    • Ohya T, Miaczynska M, Coskun U et al (2009) Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes. Nature 459:1091-1097
    • (2009) Nature , vol.459 , pp. 1091-1097
    • Ohya, T.1    Miaczynska, M.2    Coskun, U.3
  • 60
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen A, Lippe R, Christoforidis S et al (1998) EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394: 494-498
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1    Lippe, R.2    Christoforidis, S.3
  • 61
    • 0032978370 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting
    • Tall GG, Hama H, DeWald DB et al (1999) The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol Biol Cell 10:1873-1889
    • (1999) Mol Biol Cell , vol.10 , pp. 1873-1889
    • Tall, G.G.1    Hama, H.2    Dewald, D.B.3
  • 62
    • 0028816034 scopus 로고    scopus 로고
    • Grosvenor AR et al (1995) p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p
    • Sapperstein SK, Walter DM, Grosvenor AR et al (1995) p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p. Proc Natl Acad Sci U S A 92:522-526
    • Proc Natl Acad Sci U S A , vol.92 , pp. 522-526
    • Sapperstein, S.K.1    Walter, D.M.2
  • 63
    • 0028796834 scopus 로고
    • Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes
    • Barroso M, Nelson DS, Sztul E (1995) Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes. Proc Natl Acad Sci U S A 92:527-531
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 527-531
    • Barroso, M.1    Nelson, D.S.2    Sztul, E.3
  • 64
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush DR, Maurice T, Roth D et al (1996) The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 15:6483-6494
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • Terbush, D.R.1    Maurice, T.2    Roth, D.3
  • 65
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo W, Roth D, Walch-Solimena C et al (1999) The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18:1071-1080
    • (1999) EMBO J , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3
  • 66
    • 84874595708 scopus 로고    scopus 로고
    • The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes
    • Balderhaar HJ, Lachmann J, Yavavli E et al (2013) The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes. Proc Natl Acad Sci U S A 110: 3823-3828
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3823-3828
    • Balderhaar, H.J.1    Lachmann, J.2    Yavavli, E.3
  • 67
    • 77954194779 scopus 로고    scopus 로고
    • HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly
    • Hickey CM, Wickner W (2010) HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell 21:2297-2305
    • (2010) Mol Biol Cell , vol.21 , pp. 2297-2305
    • Hickey, C.M.1    Wickner, W.2
  • 68
    • 77958487311 scopus 로고    scopus 로고
    • TRAPP complexes in membrane traffic: Convergence through a common Rab
    • Barrowman J, Bhandari D, Reinisch K et al (2010) TRAPP complexes in membrane traffic: convergence through a common Rab. Nat Rev Mol Cell Biol 11:759-763
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 759-763
    • Barrowman, J.1    Bhandari, D.2    Reinisch, K.3
  • 69
    • 56149091013 scopus 로고    scopus 로고
    • The TRAPP complex: Insights into its architecture and function
    • Sacher M, Kim YG, Lavie A et al (2008) The TRAPP complex: insights into its architecture and function. Traffic 9:2032-2042
    • (2008) Traffic , vol.9 , pp. 2032-2042
    • Sacher, M.1    Kim, Y.G.2    Lavie, A.3
  • 70
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis S, McBride HM, Burgoyne RD et al (1999) The Rab5 effector EEA1 is a core component of endosome docking. Nature 397:621-625
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3
  • 71
    • 1642417606 scopus 로고    scopus 로고
    • APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment
    • Miaczynska M, Christoforidis S, Giner A et al (2004) APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. Cell 116:445-456
    • (2004) Cell , vol.116 , pp. 445-456
    • Miaczynska, M.1    Christoforidis, S.2    Giner, A.3
  • 72
    • 34547198755 scopus 로고    scopus 로고
    • Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5
    • Zhu G, Chen J, Liu J et al (2007) Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5. EMBO J 26:3484-3493
    • (2007) EMBO J , vol.26 , pp. 3484-3493
    • Zhu, G.1    Chen, J.2    Liu, J.3
  • 73
    • 42949092018 scopus 로고    scopus 로고
    • The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development
    • Schenck A, Goto-Silva L, Collinet C et al (2008) The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell 133:486-497
    • (2008) Cell , vol.133 , pp. 486-497
    • Schenck, A.1    Goto-Silva, L.2    Collinet, C.3
  • 74
    • 0033174034 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-OH kinases are Rab5 effectors
    • Christoforidis S, Miaczynska M, Ashman K et al (1999) Phosphatidylinositol-3-OH kinases are Rab5 effectors. Nat Cell Biol 1:249-252
    • (1999) Nat Cell Biol , vol.1 , pp. 249-252
    • Christoforidis, S.1    Miaczynska, M.2    Ashman, K.3
  • 75
    • 84863116629 scopus 로고    scopus 로고
    • Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function
    • Jaber N, Dou Z, Chen JS et al (2012) Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function. Proc Natl Acad Sci U S A 109:2003-2008
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 2003-2008
    • Jaber, N.1    Dou, Z.2    Chen, J.S.3
  • 76
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy bymultiple class III PI3-kinase complexes
    • Simonsen A, Tooze SA (2009) Coordination of membrane events during autophagy bymultiple class III PI3-kinase complexes. J Cell Biol 186:773-782
    • (2009) J Cell Biol , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.A.2
  • 77
    • 68249153748 scopus 로고    scopus 로고
    • Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy
    • Vergne I, Roberts E, Elmaoued RA et al (2009) Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy. EMBO J 28:2244-2258
    • (2009) EMBO J , vol.28 , pp. 2244-2258
    • Vergne, I.1    Roberts, E.2    Elmaoued, R.A.3
  • 78
    • 0242268528 scopus 로고    scopus 로고
    • Human VPS34 and p150 are Rab7 interacting partners
    • Stein MP, Feng Y, Cooper KL et al (2003) Human VPS34 and p150 are Rab7 interacting partners. Traffic 4:754-771
    • (2003) Traffic , vol.4 , pp. 754-771
    • Stein, M.P.1    Feng, Y.2    Cooper, K.L.3
  • 79
    • 84866097107 scopus 로고    scopus 로고
    • A Ypt/Rab GTPase module makes a PAS
    • Lipatova Z, Segev N (2012) A Ypt/Rab GTPase module makes a PAS. Autophagy 8:1271-1272
    • (2012) Autophagy , vol.8 , pp. 1271-1272
    • Lipatova, Z.1    Segev, N.2
  • 80
    • 77952329475 scopus 로고    scopus 로고
    • Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote autophagy
    • Lynch-Day MA, Bhandari D, Menon S et al (2010) Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote autophagy. Proc Natl Acad Sci U S A 107:7811-7816
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7811-7816
    • Lynch-Day, M.A.1    Bhandari, D.2    Menon, S.3
  • 81
    • 84878983074 scopus 로고    scopus 로고
    • Ypt1 recruits the Atg1 kinase to the preautophagosomal structure
    • Wang J, Menon S, Yamasaki A et al (2013) Ypt1 recruits the Atg1 kinase to the preautophagosomal structure. Proc Natl Acad Sci U S A 110:9800-9805
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9800-9805
    • Wang, J.1    Menon, S.2    Yamasaki, A.3
  • 82
    • 0037371509 scopus 로고    scopus 로고
    • Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot- Marie-Tooth type 2B neuropathy
    • Verhoeven K, De Jonghe P, Coen K et al (2003) Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot- Marie-Tooth type 2B neuropathy. Am J Hum Genet 72:722-727
    • (2003) Am J Hum Genet , vol.72 , pp. 722-727
    • Verhoeven, K.1    De Jonghe, P.2    Coen, K.3
  • 83
    • 4844231295 scopus 로고    scopus 로고
    • A novel RAB7 mutation associated with ulcero-mutilating neuropathy
    • Houlden H, King RH, Muddle JR et al (2004) A novel RAB7 mutation associated with ulcero-mutilating neuropathy. Ann Neurol 56:586-590
    • (2004) Ann Neurol , vol.56 , pp. 586-590
    • Houlden, H.1    King, R.H.2    Muddle, J.R.3
  • 84
    • 33750312943 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene
    • Meggouh F, Bienfait HM, Weterman MA et al (2006) Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene. Neurology 67:1476-1478
    • (2006) Neurology , vol.67 , pp. 1476-1478
    • Meggouh, F.1    Bienfait, H.M.2    Weterman, M.A.3
  • 85
    • 33745261763 scopus 로고    scopus 로고
    • Molecular genetics of autosomal-dominant axonal Charcot-Marie-Tooth disease
    • Zuchner S, Vance JM (2006) Molecular genetics of autosomal-dominant axonal Charcot-Marie-Tooth disease. Neuromol Med 8:63-74
    • (2006) Neuromol Med , vol.8 , pp. 63-74
    • Zuchner, S.1    Vance, J.M.2
  • 86
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot- Marie-Tooth type 2B disease
    • Spinosa MR, Progida C, De Luca A et al (2008) Functional characterization of Rab7 mutant proteins associated with Charcot- Marie-Tooth type 2B disease. J Neurosci 28:1640-1648
    • (2008) J Neurosci , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    De Luca, A.3
  • 87
    • 77950686629 scopus 로고    scopus 로고
    • Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation
    • McCray BA, Skordalakes E, Taylor JP (2010) Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation. Hum Mol Genet 19:1033-1047
    • (2010) Hum Mol Genet , vol.19 , pp. 1033-1047
    • McCray, B.A.1    Skordalakes, E.2    Taylor, J.P.3
  • 88
    • 34250009169 scopus 로고    scopus 로고
    • RAB23 mutations in Carpenter syndrome imply an unexpected role for hedgehog signaling in cranial-suture development and obesity
    • Jenkins D, Seelow D, Jehee FS et al (2007) RAB23 mutations in Carpenter syndrome imply an unexpected role for hedgehog signaling in cranial-suture development and obesity. Am J Hum Genet 80:1162-1170
    • (2007) Am J Hum Genet , vol.80 , pp. 1162-1170
    • Jenkins, D.1    Seelow, D.2    Jehee, F.S.3
  • 89
    • 0028224088 scopus 로고
    • Isolation of a mouse cDNA encoding Rab23, a small novel GTPase expressed predominantly in the brain
    • Olkkonen VM, Peterson JR, Dupree P et al (1994) Isolation of a mouse cDNA encoding Rab23, a small novel GTPase expressed predominantly in the brain. Gene 138:207-211
    • (1994) Gene , vol.138 , pp. 207-211
    • Olkkonen, V.M.1    Peterson, J.R.2    Dupree, P.3
  • 90
    • 0346752323 scopus 로고    scopus 로고
    • Rab23, a negative regulator of hedgehog signaling, localizes to the plasma membrane and the endocytic pathway
    • Evans TM, Ferguson C, Wainwright BJ et al (2003) Rab23, a negative regulator of hedgehog signaling, localizes to the plasma membrane and the endocytic pathway. Traffic 4:869-884
    • (2003) Traffic , vol.4 , pp. 869-884
    • Evans, T.M.1    Ferguson, C.2    Wainwright, B.J.3
  • 91
    • 0035849901 scopus 로고    scopus 로고
    • Rab23 is an essential negative regulator of the mouse Sonic hedgehog signalling pathway
    • Eggenschwiler JT, Espinoza E, Anderson KV (2001) Rab23 is an essential negative regulator of the mouse Sonic hedgehog signalling pathway. Nature 412:194-198
    • (2001) Nature , vol.412 , pp. 194-198
    • Eggenschwiler, J.T.1    Espinoza, E.2    Erson, K.V.3
  • 92
    • 0018086099 scopus 로고
    • A syndrome associating partial albinism and immunodeficiency
    • Griscelli C, Durandy A, Guy-Grand D et al (1978) A syndrome associating partial albinism and immunodeficiency. Am J Med 65: 691-702
    • (1978) Am J Med , vol.65 , pp. 691-702
    • Griscelli, C.1    Durandy, A.2    Guy-Grand, D.3
  • 93
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Menasche G, Pastural E, Feldmann J et al (2000) Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat Genet 25:173-176
    • (2000) Nat Genet , vol.25 , pp. 173-176
    • Menasche, G.1    Pastural, E.2    Feldmann, J.3
  • 94
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • Stinchcombe JC, Barral DC, Mules EH et al (2001) Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J Cell Biol 152:825-834
    • (2001) J Cell Biol , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1    Barral, D.C.2    Mules, E.H.3
  • 95
    • 0035911157 scopus 로고    scopus 로고
    • Rab27a regulates the peripheral distribution of melanosomes in melanocytes
    • Hume AN, Collinson LM, Rapak A et al (2001) Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J Cell Biol 152:795-808
    • (2001) J Cell Biol , vol.152 , pp. 795-808
    • Hume, A.N.1    Collinson, L.M.2    Rapak, A.3
  • 96
    • 0035073174 scopus 로고    scopus 로고
    • Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle
    • Wu X, Rao K, Bowers MB et al (2001) Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J Cell Sci 114:1091-1100
    • (2001) J Cell Sci , vol.114 , pp. 1091-1100
    • Wu, X.1    Rao, K.2    Bowers, M.B.3
  • 97
    • 12944255844 scopus 로고    scopus 로고
    • A mutation in Rab27a causes the vesicle transport defects observed in ashen mice
    • Wilson SM, Yip R, Swing DA et al (2000) A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc Natl Acad Sci U S A 97:7933-7938
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7933-7938
    • Wilson, S.M.1    Yip, R.2    Swing, D.A.3
  • 98
    • 21044448584 scopus 로고    scopus 로고
    • The cell biology of Hermansky-Pudlak syndrome: Recent advances
    • Di Pietro SM, Dell’Angelica EC (2005) The cell biology of Hermansky-Pudlak syndrome: recent advances. Traffic 6:525-533
    • (2005) Traffic , vol.6 , pp. 525-533
    • Di Pietro, S.M.1    Dell’angelica, E.C.2
  • 100
    • 1842556755 scopus 로고    scopus 로고
    • The rat Ruby (R) locus is Rab38: Identical mutations in Fawn-hooded and Tester-Moriyama rats derived from an ancestral Long Evans rat sub-strain
    • Oiso N, Riddle SR, Serikawa T et al (2004) The rat Ruby (R) locus is Rab38: identical mutations in Fawn-hooded and Tester-Moriyama rats derived from an ancestral Long Evans rat sub-strain. Mamm Genome 15:307-314
    • (2004) Mamm Genome , vol.15 , pp. 307-314
    • Oiso, N.1    Riddle, S.R.2    Serikawa, T.3
  • 101
    • 33750367865 scopus 로고    scopus 로고
    • Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes
    • Wasmeier C, Romao M, Plowright L et al (2006) Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes. J Cell Biol 175:271-281
    • (2006) J Cell Biol , vol.175 , pp. 271-281
    • Wasmeier, C.1    Romao, M.2    Plowright, L.3
  • 102
    • 76249116225 scopus 로고    scopus 로고
    • Mutations in the small GTPase gene RAB39B are responsible for X-linked mental retardation associated with autism, epilepsy, and macrocephaly
    • Giannandrea M, Bianchi V, Mignogna ML et al (2010) Mutations in the small GTPase gene RAB39B are responsible for X-linked mental retardation associated with autism, epilepsy, and macrocephaly. Am J Hum Genet 86:185-195
    • (2010) Am J Hum Genet , vol.86 , pp. 185-195
    • Giannandrea, M.1    Bianchi, V.2    Mignogna, M.L.3
  • 103
    • 34848816931 scopus 로고    scopus 로고
    • Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments
    • Caswell PT, Spence HJ, Parsons M et al (2007) Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments. Dev Cell 13:496-510
    • (2007) Dev Cell , vol.13 , pp. 496-510
    • Caswell, P.T.1    Spence, H.J.2    Parsons, M.3
  • 104
    • 9144271680 scopus 로고    scopus 로고
    • The RAB25 small GTPase determines aggressiveness of ovarian and breast cancers
    • Cheng KW, Lahad JP, Kuo WL et al (2004) The RAB25 small GTPase determines aggressiveness of ovarian and breast cancers. Nat Med 10:1251-1256
    • (2004) Nat Med , vol.10 , pp. 1251-1256
    • Cheng, K.W.1    Lahad, J.P.2    Kuo, W.L.3
  • 105
    • 77949756773 scopus 로고    scopus 로고
    • Loss of Rab25 promotes the development of intestinal neoplasia in mice and is associated with human colorectal adenocarcinomas
    • Nam KT, Lee HJ, Smith JJ et al (2010) Loss of Rab25 promotes the development of intestinal neoplasia in mice and is associated with human colorectal adenocarcinomas. J Clin Invest 120:840-849
    • (2010) J Clin Invest , vol.120 , pp. 840-849
    • Nam, K.T.1    Lee, H.J.2    Smith, J.J.3
  • 106
    • 84855966245 scopus 로고    scopus 로고
    • Rab25 and CLIC3 collaborate to promote integrin recycling from late endosomes/lysosomes and drive cancer progression
    • Dozynkiewicz MA, Jamieson NB, Macpherson I et al (2012) Rab25 and CLIC3 collaborate to promote integrin recycling from late endosomes/lysosomes and drive cancer progression. Dev Cell 22:131-145
    • (2012) Dev Cell , vol.22 , pp. 131-145
    • Dozynkiewicz, M.A.1    Jamieson, N.B.2    Macpherson, I.3
  • 107
    • 78049427173 scopus 로고    scopus 로고
    • Microarray analysis of hippocampal CA1 neurons implicates early endosomal dysfunction during Alzheimer’s disease progression
    • Ginsberg SD, Alldred MJ, Counts SE et al (2010) Microarray analysis of hippocampal CA1 neurons implicates early endosomal dysfunction during Alzheimer’s disease progression. Biol Psychiatry 68:885-893
    • (2010) Biol Psychiatry , vol.68 , pp. 885-893
    • Ginsberg, S.D.1    Alldred, M.J.2    Counts, S.E.3
  • 108
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer’s disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo AM, Peterhoff CM, Troncoso JC et al (2000) Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer’s disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am J Pathol 157:277-286
    • (2000) Am J Pathol , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3
  • 109
    • 84866347107 scopus 로고    scopus 로고
    • Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes
    • Chen Y, Wang Y, Zhang J et al (2012) Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes. J Cell Biol 198:545-560
    • (2012) J Cell Biol , vol.198 , pp. 545-560
    • Chen, Y.1    Wang, Y.2    Zhang, J.3
  • 110
    • 26844573782 scopus 로고    scopus 로고
    • AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain
    • Miinea CP, Sano H, Kane S et al (2005) AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain. Biochem J 391:87-93
    • (2005) Biochem J , vol.391 , pp. 87-93
    • Miinea, C.P.1    Sano, H.2    Kane, S.3
  • 111
    • 4644300287 scopus 로고    scopus 로고
    • Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160
    • Zeigerer A, McBrayer MK, McGraw TE (2004) Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160. Mol Biol Cell 15:4406-4415
    • (2004) Mol Biol Cell , vol.15 , pp. 4406-4415
    • Zeigerer, A.1    McBrayer, M.K.2    McGraw, T.E.3
  • 112
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • Sano H, Kane S, Sano E et al (2003) Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J Biol Chem 278:14599-14602
    • (2003) J Biol Chem , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.