메뉴 건너뛰기




Volumn 49, Issue 3, 2014, Pages 242-261

The ESCRT machinery: From the plasma membrane to endosomes and back again

Author keywords

Abscission; ESCRT; Intralumenal vesicle; Multivesicular endosome; Ubiquitin

Indexed keywords

ESCRT PROTEIN; UBIQUITIN;

EID: 84901851577     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2014.881777     Document Type: Review
Times cited : (106)

References (245)
  • 1
    • 0032523956 scopus 로고    scopus 로고
    • Pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis
    • Adams RR, Tavares AA, Salzberg A, et al. (1998). Pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis. Genes Dev 12:1483-94. (Pubitemid 28243633)
    • (1998) Genes and Development , vol.12 , Issue.10 , pp. 1483-1494
    • Adams, R.R.1    Tavares, A.A.M.2    Salzberg, A.3    Bellen, H.J.4    Glover, D.M.5
  • 3
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo
    • Agromayor M, Martin-Serrano J. (2006). Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. J Biol Chem 281:23083-91.
    • (2006) J Biol Chem , vol.281 , pp. 23083-23091
    • Agromayor, M.1    Martin-Serrano, J.2
  • 4
    • 84863230531 scopus 로고    scopus 로고
    • The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain
    • Agromayor M, Soler N, Caballe A, et al. (2012). The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain. Structure 20: 414-28.
    • (2012) Structure , vol.20 , pp. 414-428
    • Agromayor, M.1    Soler, N.2    Caballe, A.3
  • 6
    • 84875279930 scopus 로고    scopus 로고
    • Recruitment of UBPY and ESCRT exchange drive HD-PTP-dependent sorting of EGFR to the MVB
    • Ali N, Zhang L, Taylor S, et al. (2013). Recruitment of UBPY and ESCRT exchange drive HD-PTP-dependent sorting of EGFR to the MVB. Curr Biol 23:453-61.
    • (2013) Curr Biol , vol.23 , pp. 453-461
    • Ali, N.1    Zhang, L.2    Taylor, S.3
  • 7
    • 0033783007 scopus 로고    scopus 로고
    • Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae
    • Amerik AY, Li SJ, Hochstrasser M. (2000). Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol Chem 381:981-92.
    • (2000) Biol Chem , vol.381 , pp. 981-992
    • Amerik, A.Y.1    Li, S.J.2    Hochstrasser, M.3
  • 9
    • 78751496279 scopus 로고    scopus 로고
    • Proteomic snapshot of the EGF-induced ubiquitin network
    • doi:10.1038/ msb.2010.118
    • Argenzio E, Bange T, Oldrini B, et al. (2011). Proteomic snapshot of the EGF-induced ubiquitin network. Mol Syst Biol 7:462. doi:10.1038/ msb.2010.118.
    • (2011) Mol Syst Biol , vol.7 , pp. 462
    • Argenzio, E.1    Bange, T.2    Oldrini, B.3
  • 10
    • 36048968229 scopus 로고    scopus 로고
    • MVB-12, a fourth subunit of metazoan ESCRT-I, functions in receptor downregulation
    • Audhya A, Mcleod IX, Yates JR, Oegema K. (2007). MVB-12, a fourth subunit of metazoan ESCRT-I, functions in receptor downregulation. PLoS One 2:e956.
    • (2007) PLoS One , vol.2
    • Audhya, A.1    McLeod, I.X.2    Yates, J.R.3    Oegema, K.4
  • 11
    • 33644525938 scopus 로고    scopus 로고
    • Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1
    • Azmi I, Davies B, Dimaano C, et al. (2006). Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J Cell Biol 172:705-17.
    • (2006) J Cell Biol , vol.172 , pp. 705-717
    • Azmi, I.1    Davies, B.2    Dimaano, C.3
  • 12
    • 37749048772 scopus 로고    scopus 로고
    • ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1
    • Azmi IF, Davies BA, Xiao J, et al. (2008). ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1. Dev Cell 14: 50-61.
    • (2008) Dev Cell , vol.14 , pp. 50-61
    • Azmi, I.F.1    Davies, B.A.2    Xiao, J.3
  • 13
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, et al. (2002a). Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 3:271-82.
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3
  • 14
    • 0036697166 scopus 로고    scopus 로고
    • Endosomeassociated complex, ESCRT-Ii, recruits transport machinery for protein sorting at the multivesicular body
    • Babst M, Katzmann DJ, Snyder WB, et al. (2002b). Endosomeassociated complex, ESCRT-Ii, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 3:283-9.
    • (2002) Dev Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3
  • 15
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • DOI 10.1093/emboj/16.8.1820
    • Babst M, Sato TK, Banta LM, Emr SD. (1997). Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J 16:1820-31. (Pubitemid 27170943)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 16
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • DOI 10.1093/emboj/17.11.2982
    • Babst M, Wendland B, Estepa EJ, Emr SD. (1998). The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J 17: 2982-93. (Pubitemid 28254371)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 17
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • DOI 10.1083/jcb.200302131
    • Bache KG, Brech A, Mehlum A, Stenmark H. (2003). Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 162:435-42. (Pubitemid 36988552)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 18
    • 67650312119 scopus 로고    scopus 로고
    • Structural basis for ESCRT-III protein autoinhibition
    • Bajorek M, Schubert HL, McCullough J, et al. (2009). Structural basis for ESCRT-III protein autoinhibition. Nat Struct Mol Biol 16: 754-62.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 754-762
    • Bajorek, M.1    Schubert, H.L.2    McCullough, J.3
  • 19
    • 36249024229 scopus 로고    scopus 로고
    • Cytokinesis: Placing and making the final cut
    • DOI 10.1016/j.cell.2007.11.011, PII S0092867407014638
    • Barr FA, Gruneberg U. (2007). Cytokinesis: placing and making the final cut. Cell 131:847-60. (Pubitemid 350138092)
    • (2007) Cell , vol.131 , Issue.5 , pp. 847-860
    • Barr, F.A.1    Gruneberg, U.2
  • 21
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • DOI 10.1083/jcb.200305007
    • Bilodeau PS, Winistorfer SC, Kearney WR, et al. (2003). Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J Cell Biol 163:237-43. (Pubitemid 37363125)
    • (2003) Journal of Cell Biology , vol.163 , Issue.2 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 22
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class e vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • DOI 10.1083/jcb.200112080
    • Bishop N, Horman A, Woodman P. (2002). Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J Cell Biol 157:91-101. (Pubitemid 34847832)
    • (2002) Journal of Cell Biology , vol.157 , Issue.1 , pp. 91-101
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 23
    • 58549084391 scopus 로고    scopus 로고
    • Dictyostelium Tom1 participates to an ancestral ESCRT-0 complex
    • Blanc C, Charette SJ, Mattei S, et al. (2009). Dictyostelium Tom1 participates to an ancestral ESCRT-0 complex. Traffic 10:161-71.
    • (2009) Traffic , vol.10 , pp. 161-171
    • Blanc, C.1    Charette, S.J.2    Mattei, S.3
  • 24
    • 81155123699 scopus 로고    scopus 로고
    • Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane
    • Bodon G, Chassefeyre R, Pernet-Gallay K, et al. (2011). Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane. J Biol Chem 286: 40276-86.
    • (2011) J Biol Chem , vol.286 , pp. 40276-40286
    • Bodon, G.1    Chassefeyre, R.2    Pernet-Gallay, K.3
  • 25
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino JS, Traub LM. (2003). Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72: 395-447. (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 26
    • 84857131736 scopus 로고    scopus 로고
    • Structural basis for membrane targeting by the MVB12-associated b-prism domain of the human ESCRT-I MVB12 subunit
    • Boura E, Hurley JH. (2012). Structural basis for membrane targeting by the MVB12-associated b-prism domain of the human ESCRT-I MVB12 subunit. Proc Natl Acad Sci U S A 109:1901-6.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1901-1906
    • Boura, E.1    Hurley, J.H.2
  • 27
    • 79959371395 scopus 로고    scopus 로고
    • Solution structure of the ESCRT-I complex by small-angle X-ray scattering, Epr, and FRET spectroscopy
    • Boura E, Rózycki B, Herrick DZ, et al. (2011). Solution structure of the ESCRT-I complex by small-angle X-ray scattering, Epr, and FRET spectroscopy. Proc Natl Acad Sci U S A 108:9437-42.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9437-9442
    • Boura, E.1    Rózycki, B.2    Herrick, D.Z.3
  • 28
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class i is independent of mammalian ESCRTII
    • DOI 10.1074/jbc.M508632200
    • Bowers K, Piper SC, Edeling MA, et al. (2006). Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J Biol Chem 281:5094-105. (Pubitemid 43847775)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 29
    • 0028035094 scopus 로고
    • Myosin i localizes to the midbody region during mammalian cytokinesis
    • DOI 10.1002/cm.970290404
    • Breckler J, Burnside B. (1994). Myosin I localizes to the midbody region during mammalian cytokinesis. Cell Motil Cytoskeleton 29:312-20. (Pubitemid 24369695)
    • (1994) Cell Motility and the Cytoskeleton , vol.29 , Issue.4 , pp. 312-320
    • Breckler, J.1    Burnside, B.2
  • 30
    • 84886641339 scopus 로고    scopus 로고
    • Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation
    • Buchkovich NJ, Henne WM, Tang S, Emr SD. (2013). Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation. Dev Cell 27:201-14.
    • (2013) Dev Cell , vol.27 , pp. 201-214
    • Buchkovich, N.J.1    Henne, W.M.2    Tang, S.3    Emr, S.D.4
  • 31
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd CG, Emr SD. (1998). Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol Cell 2: 157-62. (Pubitemid 128378978)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 32
    • 84867644422 scopus 로고    scopus 로고
    • In vitro reconstitution of the ordered assembly of the endosomal sorting complex required for transport at membrane-bound HIV-1 Gag clusters
    • Carlson LA, Hurley JH. (2012). In vitro reconstitution of the ordered assembly of the endosomal sorting complex required for transport at membrane-bound HIV-1 Gag clusters. Proc Natl Acad Sci U S A 109: 16928-33.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 16928-16933
    • Carlson, L.A.1    Hurley, J.H.2
  • 33
    • 48749119362 scopus 로고    scopus 로고
    • Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release
    • Carlton JG, Agromayor M, Martin-Serrano J. (2008). Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release. Proc Natl Acad Sci U S A 105:10541-6.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10541-10546
    • Carlton, J.G.1    Agromayor, M.2    Martin-Serrano, J.3
  • 34
    • 84859630113 scopus 로고    scopus 로고
    • ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C
    • Carlton JG, Caballe A, Agromayor M, et al. (2012). ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C. Science 336:220-5.
    • (2012) Science , vol.336 , pp. 220-225
    • Carlton, J.G.1    Caballe, A.2    Agromayor, M.3
  • 35
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • DOI 10.1126/science.1143422
    • Carlton JG, Martin-Serrano J. (2007). Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316: 1908-12. (Pubitemid 47025792)
    • (2007) Science , vol.316 , Issue.5833 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 37
    • 84880883715 scopus 로고    scopus 로고
    • Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission
    • Dobro MJ, Samson RY, Yu Z, et al. (2013). Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission. Mol Biol Cell 24:2319-2327.
    • (2013) Mol Biol Cell , vol.24 , pp. 2319-2327
    • Dobro, M.J.1    Samson, R.Y.2    Yu, Z.3
  • 38
    • 0029662222 scopus 로고    scopus 로고
    • Regulation of the association of p120(cbl) with Grb2 in Jurkat T cells
    • DOI 10.1074/jbc.271.42.26369
    • Donovan JA, Ota Y, Langdon WY, Samelson LE. (1996). Regulation of the association of p120cbl with Grb2 in Jurkat T cells. J Biol Chem 271:26369-74. (Pubitemid 26347491)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 26369-26374
    • Donovan, J.A.1    Ota, Y.2    Langdon, W.Y.3    Samelson, L.E.4
  • 39
    • 42449099615 scopus 로고    scopus 로고
    • A dominant-negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes
    • DOI 10.1042/BJ20071296
    • Dukes JD, Richardson JD, Simmons R, Whitley P. (2008). A dominantnegative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes. Biochem J 411:233-9. (Pubitemid 351580175)
    • (2008) Biochemical Journal , vol.411 , Issue.2 , pp. 233-239
    • Dukes, J.D.1    Richardson, J.D.2    Simmons, R.3    Whitley, P.4
  • 40
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class i molecules
    • Duncan LM, Piper S, Dodd RB, et al. (2006). Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J 25:1635-45.
    • (2006) EMBO J , vol.25 , pp. 1635-1645
    • Duncan, L.M.1    Piper, S.2    Dodd, R.B.3
  • 41
    • 33746356163 scopus 로고    scopus 로고
    • Animal cytokinesis: From parts list to mechanisms
    • DOI 10.1146/annurev.biochem.74.082803.133425
    • Eggert US, Mitchison TJ, Field CM. (2006). Animal cytokinesis: from parts list to mechanisms. Annu Rev Biochem 75:543-66. (Pubitemid 44118043)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 543-566
    • Eggert, U.S.1    Mitchison, T.J.2    Field, C.M.3
  • 42
    • 84861167200 scopus 로고    scopus 로고
    • Computational model of cytokinetic abscission driven by ESCRT-III polymerization and remodeling
    • Elia N, Fabrikant G, Kozlov MM, Lippincott-Schwartz J. (2012). Computational model of cytokinetic abscission driven by ESCRT-III polymerization and remodeling. Biophys J 102:2309-20.
    • (2012) Biophys J , vol.102 , pp. 2309-2320
    • Elia, N.1    Fabrikant, G.2    Kozlov, M.M.3    Lippincott-Schwartz, J.4
  • 43
    • 79953225554 scopus 로고    scopus 로고
    • Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission
    • Elia N, Sougrat R, Spurlin TA, et al. (2011). Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission. Proc Natl Acad Sci U S A 108: 4846-51.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4846-4851
    • Elia, N.1    Sougrat, R.2    Spurlin, T.A.3
  • 44
    • 58149177342 scopus 로고    scopus 로고
    • Proteomic analysis of secreted membrane vesicles of archaeal Sulfolobus species reveals the presence of endosome sorting complex components
    • Ellen AF, Albers SV, Huibers W, et al. (2009). Proteomic analysis of secreted membrane vesicles of archaeal Sulfolobus species reveals the presence of endosome sorting complex components. Extremophiles 13:67-79.
    • (2009) Extremophiles , vol.13 , pp. 67-79
    • Ellen, A.F.1    Albers, S.V.2    Huibers, W.3
  • 45
    • 78349243696 scopus 로고    scopus 로고
    • Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission
    • Estey MP, Di Ciano-Oliveira C, Froese CD, et al. (2010). Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission. J Cell Biol 191:741-9.
    • (2010) J Cell Biol , vol.191 , pp. 741-749
    • Estey, M.P.1    Di Ciano-Oliveira, C.2    Froese, C.D.3
  • 46
    • 73449092185 scopus 로고    scopus 로고
    • Computational model of membrane fission catalyzed by ESCRT-III
    • Fabrikant G, Lata S, Riches JD, et al. (2009). Computational model of membrane fission catalyzed by ESCRT-III. PLoS Comput Biol 5: e1000575.
    • (2009) PLoS Comput Biol , vol.5
    • Fabrikant, G.1    Lata, S.2    Riches, J.D.3
  • 48
    • 80053206906 scopus 로고    scopus 로고
    • Association of the endosomal sorting complex ESCRT-II with the Vps20 subunit of ESCRT-III generates a curvature-sensitive complex capable of nucleating ESCRT-III filaments
    • Fyfe I, Schuh AL, Edwardson JM, Audhya A. (2011). Association of the endosomal sorting complex ESCRT-II with the Vps20 subunit of ESCRT-III generates a curvature-sensitive complex capable of nucleating ESCRT-III filaments. J Biol Chem 286:34262-70.
    • (2011) J Biol Chem , vol.286 , pp. 34262-34270
    • Fyfe, I.1    Schuh, A.L.2    Edwardson, J.M.3    Audhya, A.4
  • 50
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • DOI 10.1016/j.molcel.2005.09.014, PII S1097276505016357
    • Geetha T, Jiang J, Wooten MW. (2005). Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Mol Cell 20:301-12. (Pubitemid 41484174)
    • (2005) Molecular Cell , vol.20 , Issue.2 , pp. 301-312
    • Geetha, T.1    Jiang, J.2    Wooten, M.W.3
  • 51
    • 50849096722 scopus 로고    scopus 로고
    • Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24
    • Ghazi-Tabatabai S, Saksena S, Short JM, et al. (2008). Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24. Structure 16:1345-56.
    • (2008) Structure , vol.16 , pp. 1345-1356
    • Ghazi-Tabatabai, S.1    Saksena, S.2    Short, J.M.3
  • 53
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • Gillooly DJ, Morrow IC, Lindsay M, et al. (2000). Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J 19:4577-88.
    • (2000) EMBO J , vol.19 , pp. 4577-4588
    • Gillooly, D.J.1    Morrow, I.C.2    Lindsay, M.3
  • 54
    • 56249119525 scopus 로고    scopus 로고
    • Biochemical and structural studies of yeast Vps4 oligomerization
    • Gonciarz MD, Whitby FG, Eckert DM, et al. (2008). Biochemical and structural studies of yeast Vps4 oligomerization. J Mol Biol 384: 878-95.
    • (2008) J Mol Biol , vol.384 , pp. 878-895
    • Gonciarz, M.D.1    Whitby, F.G.2    Eckert, D.M.3
  • 55
    • 84890199269 scopus 로고    scopus 로고
    • The midbody ring scaffolds the abscission machinery in the absence of midbody microtubules
    • Green RA, Mayers JR,Wang S, et al. (2013). The midbody ring scaffolds the abscission machinery in the absence of midbody microtubules. J Cell Biol 203:505-20.
    • (2013) J Cell Biol , vol.203 , pp. 505-520
    • Green, R.A.1    Mayers, J.R.2    Wang, S.3
  • 56
    • 79953161074 scopus 로고    scopus 로고
    • Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments
    • Guizetti J, Schermelleh L, Mäntler J, et al. (2011). Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments. Science 331:1616-20.
    • (2011) Science , vol.331 , pp. 1616-1620
    • Guizetti, J.1    Schermelleh, L.2    Mäntler, J.3
  • 58
    • 84873411358 scopus 로고    scopus 로고
    • Distinct roles for β-arrestin2 and arrestin-domain-containing proteins in b2 adrenergic receptor trafficking
    • Han SO, Kommaddi RP, Shenoy SK. (2013). Distinct roles for β-arrestin2 and arrestin-domain-containing proteins in b2 adrenergic receptor trafficking. EMBO Rep 14:164-71.
    • (2013) EMBO Rep , vol.14 , pp. 164-171
    • Han, S.O.1    Kommaddi, R.P.2    Shenoy, S.K.3
  • 59
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • DOI 10.1083/jcb.200707031
    • Hanson PI, Roth R, Lin Y, Heuser JE. (2008). Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J Cell Biol 180:389-402. (Pubitemid 351185923)
    • (2008) Journal of Cell Biology , vol.180 , Issue.2 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 60
    • 40049105414 scopus 로고    scopus 로고
    • Vacuolar protein sorting: Two different functional states of the AAA-ATPase Vps4p
    • Hartmann C, Chami M, Zachariae U, et al. (2008). Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p. J Mol Biol 377:352-63.
    • (2008) J Mol Biol , vol.377 , pp. 352-363
    • Hartmann, C.1    Chami, M.2    Zachariae, U.3
  • 62
    • 84867548612 scopus 로고    scopus 로고
    • The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices
    • Henne WM, Buchkovich NJ, Zhao Y, Emr SD. (2012). The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices. Cell 151:356-71.
    • (2012) Cell , vol.151 , pp. 356-371
    • Henne, W.M.1    Buchkovich, N.J.2    Zhao, Y.3    Emr, S.D.4
  • 63
    • 84866028189 scopus 로고    scopus 로고
    • Regulation of endocytic clathrin dynamics by cargo ubiquitination
    • Henry AG, Hislop JN, Grove J, et al. (2012). Regulation of endocytic clathrin dynamics by cargo ubiquitination. Dev Cell 23:519-32.
    • (2012) Dev Cell , vol.23 , pp. 519-532
    • Henry, A.G.1    Hislop, J.N.2    Grove, J.3
  • 64
    • 79951847406 scopus 로고    scopus 로고
    • Multivesicular bodies in the enigmatic amoeboflagellate Breviata anathema and the evolution of ESCRT 0
    • Herman EK, Walker G, van der Giezen M, Dacks JB. (2011). Multivesicular bodies in the enigmatic amoeboflagellate Breviata anathema and the evolution of ESCRT 0. J Cell Sci 124:613-21.
    • (2011) J Cell Sci , vol.124 , pp. 613-621
    • Herman, E.K.1    Walker, G.2    Van Der Giezen, M.3    Dacks, J.B.4
  • 65
    • 75749137330 scopus 로고    scopus 로고
    • Recruitment of the ESCRT machinery to a putative seven-transmembrane- domain receptor is mediated by an arrestin-related protein
    • Herrador A, Herranz S, Lara D, Vincent O. (2010). Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein. Mol Cell Biol 30: 897-907.
    • (2010) Mol Cell Biol , vol.30 , pp. 897-907
    • Herrador, A.1    Herranz, S.2    Lara, D.3    Vincent, O.4
  • 66
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • DOI 10.1146/annurev.cellbio.19.110701.154617
    • Hicke L, Dunn R. (2003). Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19: 141-72. (Pubitemid 37487346)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 69
    • 33645148675 scopus 로고    scopus 로고
    • Regulation of ubiquitin-binding proteins by monoubiquitination
    • Hoeller D, Crosetto N, Blagoev B, et al. (2006). Regulation of ubiquitin-binding proteins by monoubiquitination. Nat Cell Biol 8: 163-9.
    • (2006) Nat Cell Biol , vol.8 , pp. 163-169
    • Hoeller, D.1    Crosetto, N.2    Blagoev, B.3
  • 70
    • 33751092256 scopus 로고    scopus 로고
    • CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway
    • DOI 10.1042/BJ20060897
    • Horii M, Shibata H, Kobayashi R, et al. (2006). CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway. Biochem J 400:23-32. (Pubitemid 44763816)
    • (2006) Biochemical Journal , vol.400 , Issue.1 , pp. 23-32
    • Horii, M.1    Shibata, H.2    Kobayashi, R.3    Katoh, K.4    Yorikawa, C.5    Yasuda, J.6    Maki, M.7
  • 71
    • 0034926390 scopus 로고    scopus 로고
    • CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins
    • Howard TL, Stauffer DR, Degnin CR, Hollenberg SM. (2001). CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J Cell Sci 114:2395-404. (Pubitemid 32684795)
    • (2001) Journal of Cell Science , vol.114 , Issue.13 , pp. 2395-2404
    • Howard, T.L.1    Stauffer, D.R.2    Degnin, C.R.3    Hollenberg, S.M.4
  • 72
    • 84858412262 scopus 로고    scopus 로고
    • Midbody assembly and its regulation during cytokinesis
    • Hu CK, Coughlin M, Mitchison TJ. (2012). Midbody assembly and its regulation during cytokinesis. Mol Biol Cell 23:1024-34.
    • (2012) Mol Biol Cell , vol.23 , pp. 1024-1034
    • Hu, C.K.1    Coughlin, M.2    Mitchison, T.J.3
  • 73
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • Hu Q, Milenkovic L, Jin H, et al. (2010). A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329:436-9.
    • (2010) Science , vol.329 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3
  • 74
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • DOI 10.1016/j.molcel.2006.02.018, PII S1097276506001201
    • Huang F, Kirkpatrick D, Jiang X, et al. (2006). Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell 21:737-48. (Pubitemid 43376125)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 75
    • 84884613817 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination is required for EGF receptor degradation
    • Huang F, Zeng X, Kim W, et al. (2013). Lysine 63-linked polyubiquitination is required for EGF receptor degradation. Proc Natl Acad Sci U S A 110:15722-7.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 15722-15727
    • Huang, F.1    Zeng, X.2    Kim, W.3
  • 77
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • DOI 10.1146/annurev.biophys.35.040405.102126
    • Hurley JH, Emr SD. (2006). The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu Rev Biophys Biomol Struct 35:277-98. (Pubitemid 43877379)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 78
    • 79955828987 scopus 로고    scopus 로고
    • Molecular mechanisms of ubiquitindependent membrane traffic
    • Hurley JH, Stenmark H. (2011). Molecular mechanisms of ubiquitindependent membrane traffic. Annu Rev Biophys 40:119-42.
    • (2011) Annu Rev Biophys , vol.40 , pp. 119-142
    • Hurley, J.H.1    Stenmark, H.2
  • 79
    • 44449097226 scopus 로고    scopus 로고
    • Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex
    • DOI 10.1016/j.devcel.2008.04.004, PII S1534580708001676
    • Im YJ, Hurley JH. (2008). Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. Dev Cell 14: 902-13. (Pubitemid 351766604)
    • (2008) Developmental Cell , vol.14 , Issue.6 , pp. 902-913
    • Im, Y.J.1    Hurley, J.H.2
  • 80
    • 78149426750 scopus 로고    scopus 로고
    • Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP interaction
    • Im YJ, Kuo L, Ren X, et al. (2010). Crystallographic and functional analysis of the ESCRT-I /HIV-1 Gag PTAP interaction. Structure 18: 1536-47.
    • (2010) Structure , vol.18 , pp. 1536-1547
    • Im, Y.J.1    Kuo, L.2    Ren, X.3
  • 81
    • 68449095867 scopus 로고    scopus 로고
    • Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis
    • Im YJ, Wollert T, Boura E, Hurley JH. (2009). Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev Cell 17:234-43.
    • (2009) Dev Cell , vol.17 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3    Hurley, J.H.4
  • 82
    • 84877269663 scopus 로고    scopus 로고
    • MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain
    • Iwaya N, Takasu H, Goda N, et al. (2013). MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain. J Biochem 153: 473-81.
    • (2013) J Biochem , vol.153 , pp. 473-481
    • Iwaya, N.1    Takasu, H.2    Goda, N.3
  • 83
    • 70349275158 scopus 로고    scopus 로고
    • Abnormal regulation of TSG101 in mice with spongiform neurodegeneration
    • Jiao J, Sun K, Walker WP, et al. (2009). Abnormal regulation of TSG101 in mice with spongiform neurodegeneration. Biochim Biophys Acta 1792:1027-35.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 1027-1035
    • Jiao, J.1    Sun, K.2    Walker, W.P.3
  • 84
    • 84856768251 scopus 로고    scopus 로고
    • Regulation of membrane protein degradation by starvation-response pathways
    • Jones CB, Ott EM, Keener JM, et al. (2012). Regulation of membrane protein degradation by starvation-response pathways. Traffic 13: 468-82.
    • (2012) Traffic , vol.13 , pp. 468-482
    • Jones, C.B.1    Ott, E.M.2    Keener, J.M.3
  • 85
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • DOI 10.1074/jbc.M007251200
    • Kato M, Miyazawa K, Kitamura N. (2000). A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J Biol Chem 275:37481-7. (Pubitemid 32004855)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 86
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz M, Shtiegman K, Tal-Or P, et al. (2002). Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3:740-51.
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1    Shtiegman, K.2    Tal-Or, P.3
  • 87
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • DOI 10.1016/S0092-8674(01)00434-2
    • Katzmann DJ, Babst M, Emr SD. (2001). Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106: 145-55. (Pubitemid 32772626)
    • (2001) Cell , vol.106 , Issue.2 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 88
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • DOI 10.1083/jcb.200302136
    • Katzmann DJ, Stefan CJ, Babst M, Emr SD. (2003). Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 162:413-23. (Pubitemid 36988551)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 89
    • 46049099346 scopus 로고    scopus 로고
    • Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding
    • DOI 10.1016/j.devcel.2008.05.014, PII S1534580708002396
    • Kieffer C, Skalicky JJ, Morita E, et al. (2008). Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev Cell 15:62-73. (Pubitemid 351895604)
    • (2008) Developmental Cell , vol.15 , Issue.1 , pp. 62-73
    • Kieffer, C.1    Skalicky, J.J.2    Morita, E.3    De Domenico, I.4    Ward, D.M.5    Kaplan, J.6    Sundquist, W.I.7
  • 90
    • 34247236217 scopus 로고    scopus 로고
    • Spongiform neurodegeneration-associated E3 ligase mahogunin ubiquitylates TSG101 and regulates endosomal trafficking
    • DOI 10.1091/mbc.E06-09-0787
    • Kim BY, Olzmann JA, Barsh GS, et al. (2007). Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates TSG101 and regulates endosomal trafficking. Mol Biol Cell 18: 1129-42. (Pubitemid 46626610)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.4 , pp. 1129-1142
    • Bong, Y.K.1    Olzmann, J.A.2    Barsh, G.S.3    Chin, L.-S.4    Li, L.5
  • 91
    • 0033151614 scopus 로고    scopus 로고
    • Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis
    • Komada M, Soriano P. (1999). Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev 13: 1475-85. (Pubitemid 29270251)
    • (1999) Genes and Development , vol.13 , Issue.11 , pp. 1475-1485
    • Komada, M.1    Soriano, P.2
  • 93
    • 80053564250 scopus 로고    scopus 로고
    • Midbody accumulation through evasion of autophagy contributes to cellular reprogramming and tumorigenicity
    • Kuo TC, Chen CT, Baron D, et al. (2011). Midbody accumulation through evasion of autophagy contributes to cellular reprogramming and tumorigenicity. Nat Cell Biol 13:1214-23.
    • (2011) Nat Cell Biol , vol.13 , pp. 1214-1223
    • Kuo, T.C.1    Chen, C.T.2    Baron, D.3
  • 94
    • 33846308859 scopus 로고    scopus 로고
    • Amsh, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes
    • Kyuuma M, Kikuchi K, Kojima K, et al. (2007). Amsh, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes. Cell Struct Funct 31:159-72.
    • (2007) Cell Struct Funct , vol.31 , pp. 159-172
    • Kyuuma, M.1    Kikuchi, K.2    Kojima, K.3
  • 95
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling R, Hollenberg CP. (1994). The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J 13:3261-71. (Pubitemid 24226940)
    • (1994) EMBO Journal , vol.13 , Issue.14 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 96
    • 84875519176 scopus 로고    scopus 로고
    • ESCRT-III assembly and cytokinetic abscission are induced by tension release in the intercellular bridge
    • Lafaurie-Janvore J, Maiuri P, Wang I, et al. (2013). ESCRT-III assembly and cytokinetic abscission are induced by tension release in the intercellular bridge. Science 339:1625-9.
    • (2013) Science , vol.339 , pp. 1625-1629
    • Lafaurie-Janvore, J.1    Maiuri, P.2    Wang, I.3
  • 97
    • 61449203852 scopus 로고    scopus 로고
    • Threedimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding
    • Landsberg MJ, Vajjhala PR, Rothnagel R, et al. (2009). Threedimensional structure of AAA ATPase Vps4: advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding. Structure 17:427-37.
    • (2009) Structure , vol.17 , pp. 427-437
    • Landsberg, M.J.1    Vajjhala, P.R.2    Rothnagel, R.3
  • 99
    • 41949105167 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of ESCRT-III CHMP3
    • Lata S, Roessle M, Solomons J, et al. (2008a). Structural basis for autoinhibition of ESCRT-III CHMP3. J Mol Biol 378:818-27.
    • (2008) J Mol Biol , vol.378 , pp. 818-827
    • Lata, S.1    Roessle, M.2    Solomons, J.3
  • 100
    • 51149106799 scopus 로고    scopus 로고
    • Helical structures of ESCRTIII are disassembled by VPS4
    • Lata S, Schoehn G, Jain A, et al. (2008b). Helical structures of ESCRTIII are disassembled by VPS4. Science 321:1354-7.
    • (2008) Science , vol.321 , pp. 1354-1357
    • Lata, S.1    Schoehn, G.2    Jain, A.3
  • 101
    • 54949088988 scopus 로고    scopus 로고
    • Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55
    • Lee HH, Elia N, Ghirlando R, et al. (2008). Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science 322:576-80.
    • (2008) Science , vol.322 , pp. 576-580
    • Lee, H.H.1    Elia, N.2    Ghirlando, R.3
  • 102
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • DOI 10.1016/j.cub.2007.07.029, PII S0960982207017071
    • Lee JA, Beigneux A, Ahmad ST, et al. (2007). ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr Biol 17:1561-7. (Pubitemid 47380392)
    • (2007) Current Biology , vol.17 , Issue.18 , pp. 1561-1567
    • Lee, J.-A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.-B.5
  • 103
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia
    • Lee JA, Gao FB. (2009). Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J Neurosci 29:8506-11.
    • (2009) J Neurosci , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 104
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis PA, Grinstein S. (2010). The distribution and function of phosphatidylserine in cellular membranes. Annu Rev Biophys 39: 407-27.
    • (2010) Annu Rev Biophys , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 107
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • DOI 10.1016/S0092-8674(00)81111-3
    • Li L, Cohen SN. (1996). Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell 85:319-29. (Pubitemid 26160704)
    • (1996) Cell , vol.85 , Issue.3 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 109
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitinligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin CH, Macgurn JA, Chu T, et al. (2008). Arrestin-related ubiquitinligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135:714-25.
    • (2008) Cell , vol.135 , pp. 714-725
    • Lin, C.H.1    Macgurn, J.A.2    Chu, T.3
  • 111
    • 62149111407 scopus 로고    scopus 로고
    • Sensing chromosome biorientation by spatial separation of aurora B kinase from kinetochore substrates
    • Liu D, Vader G, Vromans MJ, et al. (2009). Sensing chromosome biorientation by spatial separation of aurora B kinase from kinetochore substrates. Science 323:1350-3.
    • (2009) Science , vol.323 , pp. 1350-1353
    • Liu, D.1    Vader, G.2    Vromans, M.J.3
  • 113
    • 38049091552 scopus 로고    scopus 로고
    • 3D reconstruction of mammalian septin filaments
    • Lukoyanova N, Baldwin SA, Trinick J. (2008). 3D reconstruction of mammalian septin filaments. J Mol Biol 376:1-7.
    • (2008) J Mol Biol , vol.376 , pp. 1-7
    • Lukoyanova, N.1    Baldwin, S.A.2    Trinick, J.3
  • 116
    • 77957130448 scopus 로고    scopus 로고
    • Evolution of diverse cell division and vesicle formation systems in Archaea
    • Makarova KS, Yutin N, Bell SD, Koonin EV. (2010). Evolution of diverse cell division and vesicle formation systems in Archaea. Nat Rev Microbiol 8:731-41.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 731-741
    • Makarova, K.S.1    Yutin, N.2    Bell, S.D.3    Koonin, E.V.4
  • 117
    • 35348847143 scopus 로고    scopus 로고
    • Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation
    • DOI 10.1111/j.1600-0854.2007.00630.x
    • Malerød L, Stuffers S, Brech A, Stenmark H. (2007). Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation. Traffic 8: 1617-29. (Pubitemid 47578365)
    • (2007) Traffic , vol.8 , Issue.11 , pp. 1617-1629
    • Malerod, L.1    Stuffers, S.2    Brech, A.3    Stenmark, H.4
  • 118
    • 77954626403 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4
    • Malik R, Marchese A. (2010). Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4. Mol Biol Cell 21:2529-41.
    • (2010) Mol Biol Cell , vol.21 , pp. 2529-2541
    • Malik, R.1    Marchese, A.2
  • 119
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao Y, Nickitenko A, Duan X, et al. (2000). Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 100:447-56.
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.1    Nickitenko, A.2    Duan, X.3
  • 120
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • DOI 10.1016/S1534-5807(03)00321-6, PII S1534580703003216
    • Marchese A, Raiborg C, Santini F, et al. (2003). The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev Cell 5:709-22. (Pubitemid 37362215)
    • (2003) Developmental Cell , vol.5 , Issue.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 121
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • DOI 10.1128/JVI.77.8.4794-4804.2003
    • Martin-Serrano J, Zang T, Bieniasz PD. (2003). Role of ESCRT-I in retroviral budding. J Virol 77:4794-804. (Pubitemid 36402829)
    • (2003) Journal of Virology , vol.77 , Issue.8 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 122
    • 84860294382 scopus 로고    scopus 로고
    • CC2D1A is a regulator of ESCRT-III CHMP4B
    • Martinelli N, Hartlieb B, Usami Y, et al. (2012). CC2D1A is a regulator of ESCRT-III CHMP4B. J Mol Biol 419:75-88.
    • (2012) J Mol Biol , vol.419 , pp. 75-88
    • Martinelli, N.1    Hartlieb, B.2    Usami, Y.3
  • 123
    • 79953220455 scopus 로고    scopus 로고
    • ESCRT-0 assembles as a heterotetrameric complex on membranes and binds multiple ubiquitinylated cargoes simultaneously
    • Mayers JR, Fyfe I, Schuh AL, et al. (2011). ESCRT-0 assembles as a heterotetrameric complex on membranes and binds multiple ubiquitinylated cargoes simultaneously. J Biol Chem 286:9636-45.
    • (2011) J Biol Chem , vol.286 , pp. 9636-9645
    • Mayers, J.R.1    Fyfe, I.2    Schuh, A.L.3
  • 124
    • 84880393706 scopus 로고    scopus 로고
    • Regulation of ubiquitindependent cargo sorting by multiple endocytic adaptors at the plasma membrane
    • Mayers JR, Wang L, Pramanik J, et al. (2013). Regulation of ubiquitindependent cargo sorting by multiple endocytic adaptors at the plasma membrane. Proc Natl Acad Sci U S A 110:11857-62.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 11857-11862
    • Mayers, J.R.1    Wang, L.2    Pramanik, J.3
  • 125
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosomeassociated ubiquitin isopeptidase
    • McCullough J, Clague MJ, Urbé S. (2004). AMSH is an endosomeassociated ubiquitin isopeptidase. J Cell Biol 166:487-92.
    • (2004) J Cell Biol , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbé, S.3
  • 126
    • 84878951746 scopus 로고    scopus 로고
    • Membrane fission reactions of the mammalian ESCRT pathway
    • McCullough J, Colf LA, Sundquist WI. (2013). Membrane fission reactions of the mammalian ESCRT pathway. Annu Rev Biochem 82: 663-92.
    • (2013) Annu Rev Biochem , vol.82 , pp. 663-692
    • McCullough, J.1    Colf, L.A.2    Sundquist, W.I.3
  • 128
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • DOI 10.1016/j.cub.2005.11.073, PII S0960982205015241
    • McCullough J, Row PE, Lorenzo O, et al. (2006). Activation of the endosome-associated ubiquitin isopeptidase AMSH by Stam, a component of the multivesicular body-sorting machinery. Curr Biol 16:160-5. (Pubitemid 43117430)
    • (2006) Current Biology , vol.16 , Issue.2 , pp. 160-165
    • McCullough, J.1    Row, P.E.2    Lorenzo, O.3    Doherty, M.4    Beynon, R.5    Clague, M.J.6    Urbe, S.7
  • 129
    • 39449131442 scopus 로고    scopus 로고
    • Regulation of Tsg101 expression by the steadiness box: A role of Tsg101-associated ligase
    • DOI 10.1091/mbc.E07-09-0957
    • McDonald B, Martin-Serrano J. (2008). Regulation of Tsg101 expression by the steadiness box: a role of Tsg101-associated ligase. Mol Biol Cell 19:754-63. (Pubitemid 351272162)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 754-763
    • McDonald, B.1    Martin-Serrano, J.2
  • 130
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • DOI 10.1038/nature04396
    • McMahon HT, Gallop JL. (2005). Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438:590-6. (Pubitemid 41740562)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 131
    • 80052706416 scopus 로고    scopus 로고
    • Genetic interactions with mutations affecting septin assembly reveal ESCRT functions in budding yeast cytokinesis
    • McMurray MA, Stefan CJ, Wemmer M, et al. (2011). Genetic interactions with mutations affecting septin assembly reveal ESCRT functions in budding yeast cytokinesis. Biol Chem 392:699-712.
    • (2011) Biol Chem , vol.392 , pp. 699-712
    • McMurray, M.A.1    Stefan, C.J.2    Wemmer, M.3
  • 132
    • 78649829353 scopus 로고    scopus 로고
    • ERBB2 is a target for USP8- mediated deubiquitination
    • Meijer IM, van Leeuwen JE. (2011). ERBB2 is a target for USP8- mediated deubiquitination. Cell Signal 23:458-67.
    • (2011) Cell Signal , vol.23 , pp. 458-467
    • Meijer, I.M.1    Van Leeuwen, J.E.2
  • 133
    • 0028885860 scopus 로고
    • Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor
    • Meisner H, Czech MP. (1995). Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor. J Biol Chem 270: 25332-5.
    • (1995) J Biol Chem , vol.270 , pp. 25332-25335
    • Meisner, H.1    Czech, M.P.2
  • 134
    • 84872112730 scopus 로고    scopus 로고
    • Wrapping up the bad news: HIV assembly and release
    • doi:10.1186/1742-4690
    • Meng B, Lever AM. (2013). Wrapping up the bad news: HIV assembly and release. Retrovirology 10:5. doi:10.1186/1742-4690- 10-5.
    • (2013) Retrovirology , vol.10 , Issue.5 , pp. 10-15
    • Meng, B.1    Lever, A.M.2
  • 135
    • 78149276258 scopus 로고    scopus 로고
    • Activation of human VPS4A by ESCRTIII proteins reveals ability of substrates to relieve enzyme autoinhibition
    • Merrill SA, Hanson PI. (2010). Activation of human VPS4A by ESCRTIII proteins reveals ability of substrates to relieve enzyme autoinhibition. J Biol Chem 285:35428-38.
    • (2010) J Biol Chem , vol.285 , pp. 35428-35438
    • Merrill, S.A.1    Hanson, P.I.2
  • 136
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • DOI 10.1016/S0092-8674(00)80776-X
    • Misra S, Hurley JH. (1999). Crystal structure of a phosphatidylinositol 3- phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97:657-66. (Pubitemid 29256968)
    • (1999) Cell , vol.97 , Issue.5 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 137
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes
    • DOI 10.1091/mbc.E05-06-0560
    • Mizuno E, Iura T, Mukai A, et al. (2005). Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol Biol Cell 16:5163-74. (Pubitemid 41566829)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 138
    • 0141744750 scopus 로고    scopus 로고
    • STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif
    • DOI 10.1091/mbc.E02-12-0823
    • Mizuno E, Kawahata K, Kato M, et al. (2003). STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif. Mol Biol Cell 14:3675-89. (Pubitemid 37151618)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.9 , pp. 3675-3689
    • Mizuno, E.1    Kawahata, K.2    Kato, M.3    Kitamura, N.4    Komada, M.5
  • 139
    • 84892543174 scopus 로고    scopus 로고
    • The oligomeric state of the active Vps4 AAA ATPase
    • [Epub ahead of print]. doi: 10.1016/j.jmb.2013.09.043
    • Monroe N, Han H, Gonciarz MD, et al. (2013). The oligomeric state of the active Vps4 AAA ATPase. J Mol Biol [Epub ahead of print]. doi: 10.1016/j.jmb.2013.09.043.
    • J Mol Biol , vol.2013
    • Monroe, N.1    Han, H.2    Gonciarz, M.D.3
  • 140
    • 77955618368 scopus 로고    scopus 로고
    • Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance
    • Morita E, Colf LA, Karren MA, et al. (2010). Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. Proc Natl Acad Sci U S A 107:12889-94.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12889-12894
    • Morita, E.1    Colf, L.A.2    Karren, M.A.3
  • 141
    • 34347339528 scopus 로고    scopus 로고
    • Identification of Human MVB12 Proteins as ESCRT-I Subunits that Function in HIV Budding
    • DOI 10.1016/j.chom.2007.06.003, PII S1931312807001291
    • Morita E, Sandrin V, Alam SL, et al. (2007a). Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding. Cell Host Microbe 2:41-53. (Pubitemid 47010242)
    • (2007) Cell Host and Microbe , vol.2 , Issue.1 , pp. 41-53
    • Morita, E.1    Sandrin, V.2    Alam, S.L.3    Eckert, D.M.4    Gygi, S.P.5    Sundquist, W.I.6
  • 142
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • DOI 10.1038/sj.emboj.7601850, PII 7601850
    • Morita E, Sandrin V, Chung HY, et al. (2007b). Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J 26:4215-27. (Pubitemid 47525161)
    • (2007) EMBO Journal , vol.26 , Issue.19 , pp. 4215-4227
    • Morita, E.1    Sandrin, V.2    Chung, H.-Y.3    Morham, S.G.4    Gygi, S.P.5    Rodesch, C.K.6    Sundquist, W.I.7
  • 143
    • 79952640255 scopus 로고    scopus 로고
    • ESCRT-III protein requirements for HIV-1 budding
    • Morita E, Sandrin V, McCullough J, et al. (2011). ESCRT-III protein requirements for HIV-1 budding. Cell Host Microbe 9:235-42.
    • (2011) Cell Host Microbe , vol.9 , pp. 235-242
    • Morita, E.1    Sandrin, V.2    McCullough, J.3
  • 144
    • 0020377448 scopus 로고
    • Isolation and initial characterization of the mammalian midbody
    • DOI 10.1083/jcb.94.3.654
    • Mullins JM, Mcintosh Jr. (1982). Isolation and initial characterization of the mammalian midbody. J Cell Biol 94:654-61. (Pubitemid 13241197)
    • (1982) Journal of Cell Biology , vol.94 , Issue.3 , pp. 654-661
    • Mullins, J.M.1    McIntosh, J.R.2
  • 146
    • 77949465181 scopus 로고    scopus 로고
    • Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles
    • Nickerson DP, West M, Henry R, Odorizzi G. (2010). Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol Biol Cell 21: 1023-32.
    • (2010) Mol Biol Cell , vol.21 , pp. 1023-1032
    • Nickerson, D.P.1    West, M.2    Henry, R.3    Odorizzi, G.4
  • 147
    • 84883720423 scopus 로고    scopus 로고
    • Relief of autoinhibition enhances Vta1 activation of Vps4 via the Vps4 stimulatory element
    • Norgan AP, Davies BA, Azmi IF, et al. (2013). Relief of autoinhibition enhances Vta1 activation of Vps4 via the Vps4 stimulatory element. J Biol Chem 288:26147-56.
    • (2013) J Biol Chem , vol.288 , pp. 26147-26156
    • Norgan, A.P.1    Davies, B.A.2    Azmi, I.F.3
  • 148
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • DOI 10.1038/nature06171, PII NATURE06171
    • Obita T, Saksena S, Ghazi-Tabatabai S, et al. (2007). Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449:735-9. (Pubitemid 47552090)
    • (2007) Nature , vol.449 , Issue.7163 , pp. 735-739
    • Obita, T.1    Saksena, S.2    Ghazi-Tabatabai, S.3    Gill, D.J.4    Perisic, O.5    Emr, S.D.6    Williams, R.L.7
  • 149
    • 80755132190 scopus 로고    scopus 로고
    • Endosomal transport via ubiquitination
    • Piper RC, Lehner PJ. (2011). Endosomal transport via ubiquitination. Trends Cell Biol 21:647-55.
    • (2011) Trends Cell Biol , vol.21 , pp. 647-655
    • Piper, R.C.1    Lehner, P.J.2
  • 150
    • 66749147856 scopus 로고    scopus 로고
    • A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments
    • Pires R, Hartlieb B, Signor L, et al. (2009). A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure 17:843-56.
    • (2009) Structure , vol.17 , pp. 843-856
    • Pires, R.1    Hartlieb, B.2    Signor, L.3
  • 151
    • 39749202339 scopus 로고    scopus 로고
    • Final stages of cytokinesis and midbody ring formation are controlled by BRUCE
    • DOI 10.1016/j.cell.2008.01.012, PII S0092867408001128
    • Pohl C, Jentsch S. (2008). Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. Cell 132:832-45. (Pubitemid 351312799)
    • (2008) Cell , vol.132 , Issue.5 , pp. 832-845
    • Pohl, C.1    Jentsch, S.2
  • 156
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano R, Bonifacino JS. (2004). Interactions of GGA3 with the ubiquitin sorting machinery. Nat Cell Biol 6:244-51. (Pubitemid 38344363)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 160
    • 38849164882 scopus 로고    scopus 로고
    • Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking
    • DOI 10.1016/j.yexcr.2007.10.014, PII S0014482707004909
    • Raiborg C, Malerød L, Pedersen NM, Stenmark H. (2008). Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking. Exp Cell Res 314:801-13. (Pubitemid 351191901)
    • (2008) Experimental Cell Research , vol.314 , Issue.4 , pp. 801-813
    • Raiborg, C.1    Malerod, L.2    Pedersen, N.M.3    Stenmark, H.4
  • 161
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg C, Stenmark H. (2009). The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458:445-52.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 162
    • 79952588626 scopus 로고    scopus 로고
    • Multiple interactions between the ESCRT machinery and arrestin-related proteins: Implications for PPXY-dependent budding
    • Rauch S, Martin-Serrano J. (2011). Multiple interactions between the ESCRT machinery and arrestin-related proteins: implications for PPXY-dependent budding. J Virol 85:3546-56.
    • (2011) J Virol , vol.85 , pp. 3546-3556
    • Rauch, S.1    Martin-Serrano, J.2
  • 163
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class e vps mutants
    • Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH. (1992). Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 3:1389-402. (Pubitemid 23091465)
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.12 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 164
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
    • DOI 10.1093/emboj/20.18.5176
    • Reggiori F, Pelham HR. (2001). Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J 20: 5176-86. (Pubitemid 32910912)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.B.2
  • 165
    • 33846137688 scopus 로고    scopus 로고
    • Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies
    • DOI 10.1091/mbc.E06-06-0557
    • Ren J, Kee Y, Huibregtse JM, Piper RC. (2007). Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol Biol Cell 18:324-35. (Pubitemid 46074967)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.1 , pp. 324-335
    • Ren, J.1    Kee, Y.2    Huibregtse, J.M.3    Piper, R.C.4
  • 166
    • 77949567362 scopus 로고    scopus 로고
    • VHS domains of ESCRT-0 cooperate in highavidity binding to polyubiquitinated cargo
    • Ren X, Hurley JH. (2010). VHS domains of ESCRT-0 cooperate in highavidity binding to polyubiquitinated cargo. EMBO J 29:1045-54.
    • (2010) EMBO J , vol.29 , pp. 1045-1054
    • Ren, X.1    Hurley, J.H.2
  • 167
    • 85027934034 scopus 로고    scopus 로고
    • Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast
    • Ren X, Hurley JH. (2011). Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast. EMBO J 30:2130-9.
    • (2011) EMBO J , vol.30 , pp. 2130-2139
    • Ren, X.1    Hurley, J.H.2
  • 168
    • 61749093376 scopus 로고    scopus 로고
    • Hybrid structural model of the complete human ESCRT-0 complex
    • Ren X, Kloer DP, Kim YC, et al. (2009). Hybrid structural model of the complete human ESCRT-0 complex. Structure 17:406-16.
    • (2009) Structure , vol.17 , pp. 406-416
    • Ren, X.1    Kloer, D.P.2    Kim, Y.C.3
  • 169
    • 34249073136 scopus 로고    scopus 로고
    • Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies
    • DOI 10.1038/sj.emboj.7601692, PII 7601692
    • Richter C, West M, Odorizzi G. (2007). Dual mechanisms specify Doa4- mediated deubiquitination at multivesicular bodies. EMBO J 26: 2454-64. (Pubitemid 46788318)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2454-2464
    • Richter, C.1    West, M.2    Odorizzi, G.3
  • 170
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder SE, Banta LM, Köhrer K, et al. (1996). Multilamellar endosomelike compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol Biol Cell 7:985-99. (Pubitemid 26181732)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.6 , pp. 985-999
    • Rieder, S.E.1    Banta, L.M.2    Kohrer, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 171
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak A, Vale RD. (2008). Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451:363-7.
    • (2008) Nature , vol.451 , pp. 363-367
    • Roll-Mecak, A.1    Vale, R.D.2
  • 172
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman JS, Jing X, Leser GP, Lamb RA. (2010). Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142: 902-13.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 174
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • DOI 10.1074/jbc.M512615200
    • Row PE, Prior IA, McCullough J, et al. (2006). The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J Biol Chem 281:12618-24. (Pubitemid 43855351)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 175
    • 39449140052 scopus 로고    scopus 로고
    • Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting
    • DOI 10.1091/mbc.E07-07-0694
    • Rue SM, Mattei S, Saksena S, Emr SD. (2008). Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell 19:475-84. (Pubitemid 351272137)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 475-484
    • Rue, S.M.1    Mattei, S.2    Saksena, S.3    Emr, S.D.4
  • 176
    • 84866265657 scopus 로고    scopus 로고
    • Class e compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase
    • Russell MR, Shideler T, Nickerson DP, et al. (2012). Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the
    • (2012) J Cell Sci , vol.125 , pp. 5208-5220
    • Russell, M.R.1    Shideler, T.2    Nickerson, D.P.3
  • 178
    • 36248991778 scopus 로고    scopus 로고
    • ESCRTing proteins in the endocytic pathway
    • DOI 10.1016/j.tibs.2007.09.010, PII S0968000407002617
    • Saksena S, Sun J, Chu T, Emr SD. (2007). ESCRTing proteins in the endocytic pathway. Trends Biochem Sci 32:561-73. (Pubitemid 350123053)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.12 , pp. 561-573
    • Saksena, S.1    Sun, J.2    Chu, T.3    Emr, S.D.4
  • 179
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • Saksena S, Wahlman J, Teis D, et al. (2009). Functional reconstitution of ESCRT-III assembly and disassembly. Cell 136:97-109.
    • (2009) Cell , vol.136 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3
  • 180
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • Samson RY, Obita T, Freund SM, et al. (2008). A role for the ESCRT system in cell division in archaea. Science 322:1710-3.
    • (2008) Science , vol.322 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3
  • 181
    • 78651468723 scopus 로고    scopus 로고
    • Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division
    • Samson RY, Obita T, Hodgson B, et al. (2011). Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division. Mol Cell 41:186-96.
    • (2011) Mol Cell , vol.41 , pp. 186-196
    • Samson, R.Y.1    Obita, T.2    Hodgson, B.3
  • 182
    • 84885099846 scopus 로고    scopus 로고
    • ESCRT requirements for EIAV budding
    • doi: 10.1186/1742-4690-10-104
    • Sandrin V, Sundquist WI. (2013). ESCRT requirements for EIAV budding. Retrovirology 10:104. doi: 10.1186/1742-4690-10-104.
    • (2013) Retrovirology , vol.10 , pp. 104
    • Sandrin, V.1    Sundquist, W.I.2
  • 183
    • 0024433443 scopus 로고
    • Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells
    • Sanger JM, Mittal B, Dome JS, Sanger JW. (1989). Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells. Cell Motil Cytoskeleton 14:201-19. (Pubitemid 19272136)
    • (1989) Cell Motility and the Cytoskeleton , vol.14 , Issue.2 , pp. 201-219
    • Sanger, J.M.1    Mittal, B.2    Dome, J.S.3    Sanger, J.W.4
  • 184
    • 0023575751 scopus 로고
    • Interzone microtubule behavior in late anaphase and telophase spindles
    • Saxton WM, Mcintosh Jr. (1987). Interzone microtubule behavior in late anaphase and telophase spindles. J Cell Biol 105:875-86. (Pubitemid 18043847)
    • (1987) Journal of Cell Biology , vol.105 , Issue.2 , pp. 875-886
    • Saxton, W.M.1    McIntosh, J.R.2
  • 189
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination
    • DOI 10.1074/jbc.M209626200
    • Shenoy SK, Lefkowitz RJ. (2003). Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of betaarrestin deubiquitination. J Biol Chem 278:14498-506. (Pubitemid 36800003)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 190
    • 52049117442 scopus 로고    scopus 로고
    • Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor
    • Shenoy SK, Xiao K, Venkataramanan V, et al. (2008). Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor. J Biol Chem 283: 22166-76.
    • (2008) J Biol Chem , vol.283 , pp. 22166-22176
    • Shenoy, S.K.1    Xiao, K.2    Venkataramanan, V.3
  • 192
    • 65349101661 scopus 로고    scopus 로고
    • ESCRT ubiquitinbinding domains function cooperatively during MVB cargo sorting
    • Shields SB, Oestreich AJ, Winistorfer S, et al. (2009). ESCRT ubiquitinbinding domains function cooperatively during MVB cargo sorting. J Cell Biol 185:213-24.
    • (2009) J Cell Biol , vol.185 , pp. 213-224
    • Shields, S.B.1    Oestreich, A.J.2    Winistorfer, S.3
  • 193
    • 80052621127 scopus 로고    scopus 로고
    • How ubiquitin functions with ESCRTs
    • Shields SB, Piper RC. (2011). How ubiquitin functions with ESCRTs. Traffic 12:1306-17.
    • (2011) Traffic , vol.12 , pp. 1306-1317
    • Shields, S.B.1    Piper, R.C.2
  • 195
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • DOI 10.1038/ncb790
    • Shih SC, Katzmann DJ, Schnell JD, et al. (2002). Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 4:389-93. (Pubitemid 34521036)
    • (2002) Nature Cell Biology , vol.4 , Issue.5 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 196
    • 33645325937 scopus 로고    scopus 로고
    • CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis
    • Shim JH, Xiao C, Hayden MS, et al. (2006). CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis. J Cell Biol 172:1045-56.
    • (2006) J Cell Biol , vol.172 , pp. 1045-1056
    • Shim, J.H.1    Xiao, C.2    Hayden, M.S.3
  • 197
    • 34447527768 scopus 로고    scopus 로고
    • Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain
    • DOI 10.1111/j.1600-0854.2007.00584.x
    • Shim S, Kimpler LA, Hanson PI. (2007). Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 8:1068-79. (Pubitemid 47074039)
    • (2007) Traffic , vol.8 , Issue.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 198
    • 46049118283 scopus 로고    scopus 로고
    • Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly
    • Shim S, Merrill SA, Hanson PI. (2008). Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly. Mol Biol Cell 19:2661-72.
    • (2008) Mol Biol Cell , vol.19 , pp. 2661-2672
    • Shim, S.1    Merrill, S.A.2    Hanson, P.I.3
  • 199
    • 84871586331 scopus 로고    scopus 로고
    • Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport
    • Skalicky JJ, Arii J, Wenzel DM, et al. (2012). Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport. J Biol Chem 287:43910-26.
    • (2012) J Biol Chem , vol.287 , pp. 43910-43926
    • Skalicky, J.J.1    Arii, J.2    Wenzel, D.M.3
  • 201
    • 80051495469 scopus 로고    scopus 로고
    • Structural basis for ESCRT-III CHMP3 recruitment of AMSH
    • Solomons J, Sabin C, Poudevigne E, et al. (2011). Structural basis for ESCRT-III CHMP3 recruitment of AMSH. Structure 19:1149-59.
    • (2011) Structure , vol.19 , pp. 1149-1159
    • Solomons, J.1    Sabin, C.2    Poudevigne, E.3
  • 203
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • DOI 10.1074/jbc.M201106200
    • Stahelin RV, Long F, Diraviyam K, et al. (2002). Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J Biol Chem 277:26379-88. (Pubitemid 34967131)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6
  • 204
    • 79960740814 scopus 로고    scopus 로고
    • UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting
    • Stefani F, Zhang L, Taylor S, et al. (2011). UBAP1 is a component of an endosome-specific ESCRT-I complex that is essential for MVB sorting. Curr Biol 21:1245-50.
    • (2011) Curr Biol , vol.21 , pp. 1245-1250
    • Stefani, F.1    Zhang, L.2    Taylor, S.3
  • 205
    • 70350343134 scopus 로고    scopus 로고
    • Cytokinetic abscission: Cellular dynamics at the midbody
    • Steigemann P, Gerlich DW. (2009). Cytokinetic abscission: cellular dynamics at the midbody. Trends Cell Biol 19:606-16.
    • (2009) Trends Cell Biol , vol.19 , pp. 606-616
    • Steigemann, P.1    Gerlich, D.W.2
  • 207
    • 78951480972 scopus 로고    scopus 로고
    • A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination
    • Stringer DK, Piper RC. (2011). A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination. J Cell Biol 192:229-42.
    • (2011) J Cell Biol , vol.192 , pp. 229-242
    • Stringer, D.K.1    Piper, R.C.2
  • 210
    • 0033516556 scopus 로고    scopus 로고
    • Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines
    • Tanaka N, Kaneko K, Asao H, et al. (1999). Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines. J Biol Chem 274:19129-35.
    • (1999) J Biol Chem , vol.274 , pp. 19129-19135
    • Tanaka, N.1    Kaneko, K.2    Asao, H.3
  • 211
    • 53249131094 scopus 로고    scopus 로고
    • Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation
    • Teis D, Saksena S, Emr SD. (2008). Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Dev Cell 15:578-89.
    • (2008) Dev Cell , vol.15 , pp. 578-589
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 212
    • 77649335931 scopus 로고    scopus 로고
    • ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation
    • Teis D, Saksena S, Judson BL, Emr SD. (2010). ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation. EMBO J 29:871-83.
    • (2010) EMBO J , vol.29 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3    Emr, S.D.4
  • 213
    • 33645981584 scopus 로고    scopus 로고
    • ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes
    • Teo H, Gill DJ, Sun J, et al. (2006). ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes. Cell 125:99-111.
    • (2006) Cell , vol.125 , pp. 99-111
    • Teo, H.1    Gill, D.J.2    Sun, J.3
  • 214
    • 5044245523 scopus 로고    scopus 로고
    • ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes
    • DOI 10.1016/j.devcel.2004.09.003, PII S1534580704003235
    • Teo H, Perisic O, González B, Williams RL. (2004). ESCRT-Ii, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. Dev Cell 7:559-69. (Pubitemid 39341841)
    • (2004) Developmental Cell , vol.7 , Issue.4 , pp. 559-569
    • Teo, H.1    Perisic, O.2    Gonzalez, B.3    Williams, R.L.4
  • 215
    • 27644498439 scopus 로고    scopus 로고
    • Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila
    • DOI 10.1016/j.devcel.2005.09.020, PII S1534580705003825
    • Thompson BJ, Mathieu J, Sung HH, et al. (2005). Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila. Dev Cell 9:711-20. (Pubitemid 41555152)
    • (2005) Developmental Cell , vol.9 , Issue.5 , pp. 711-720
    • Thompson, B.J.1    Mathieu, J.2    Sung, H.-H.3    Loeser, E.4    Rorth, P.5    Cohen, S.M.6
  • 216
    • 33747795207 scopus 로고    scopus 로고
    • A systematic analysis of human CHMP protein interactions: Additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex
    • DOI 10.1016/j.ygeno.2006.04.003, PII S0888754306001121
    • Tsang HT, Connell JW, Brown SE, et al. (2006). A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. Genomics 88:333-46. (Pubitemid 44278530)
    • (2006) Genomics , vol.88 , Issue.3 , pp. 333-346
    • Tsang, H.T.H.1    Connell, J.W.2    Brown, S.E.3    Thompson, A.4    Reid, E.5    Sanderson, C.M.6
  • 217
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • DOI 10.1034/j.1600-0854.2001.20905.x
    • Urbanowski JL, Piper RC. (2001). Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2:622-30. (Pubitemid 32825701)
    • (2001) Traffic , vol.2 , Issue.9 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 218
    • 0033800735 scopus 로고    scopus 로고
    • Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine kinase substrate
    • Urbé, S., Mills IG, Stenmark H, et al. (2000). Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine kinase substrate. Mol Cell Biol 20:7685-92.
    • (2000) Mol Cell Biol , vol.20 , pp. 7685-7692
    • Urbé, S.1    Mills, I.G.2    Stenmark, H.3
  • 219
    • 27644568520 scopus 로고    scopus 로고
    • The Drosophila tumor suppressor vps25 prevents nonautonomous overproliferation by tegulating Notch trafficking
    • DOI 10.1016/j.devcel.2005.09.019, PII S1534580705003813
    • Vaccari T, Bilder D. (2005). The Drosophila tumor suppressor vps25 prevents nonautonomous overproliferation by regulating notch trafficking. Dev Cell 9:687-98. (Pubitemid 41555150)
    • (2005) Developmental Cell , vol.9 , Issue.5 , pp. 687-698
    • Vaccari, T.1    Bilder, D.2
  • 220
  • 221
  • 223
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • DOI 10.1093/emboj/21.3.303
    • Waterman H, Katz M, Rubin C, et al. (2002). A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J 21:303-13. (Pubitemid 34137292)
    • (2002) EMBO Journal , vol.21 , Issue.3 , pp. 303-313
    • Waterman, H.1    Katz, M.2    Rubin, C.3    Shtiegman, K.4    Lavi, S.5    Elson, A.6    Jovin, T.7    Yarden, Y.8
  • 224
    • 0033529537 scopus 로고    scopus 로고
    • The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman H, Levkowitz G, Alroy I, Yarden Y. (1999). The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J Biol Chem 274:22151-4.
    • (1999) J Biol Chem , vol.274 , pp. 22151-22154
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 225
    • 76949098165 scopus 로고    scopus 로고
    • Ultrastructural characterization of giant endosomes induced by GTPase-deficient Rab5
    • Wegner CS, Wegener CS, Malerød L, et al. (2010). Ultrastructural characterization of giant endosomes induced by GTPase-deficient Rab5. Histochem Cell Biol 133:41-55.
    • (2010) Histochem Cell Biol , vol.133 , pp. 41-55
    • Wegner, C.S.1    Wegener, C.S.2    Malerød, L.3
  • 227
    • 33947713961 scopus 로고    scopus 로고
    • Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing
    • DOI 10.1083/jcb.200610072
    • White SR, Evans KJ, Lary J, et al. (2007). Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing. J Cell Biol 176:995-1005. (Pubitemid 46506972)
    • (2007) Journal of Cell Biology , vol.176 , Issue.7 , pp. 995-1005
    • White, S.R.1    Evans, K.J.2    Lary, J.3    Cole, J.L.4    Lauring, B.5
  • 228
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • DOI 10.1083/jcb.126.4.945
    • Whiteheart SW, Rossnagel K, Buhrow SA, et al. (1994). N-ethylmaleimide- sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J Cell Biol 126:945-54. (Pubitemid 24252141)
    • (1994) Journal of Cell Biology , vol.126 , Issue.4 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 229
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • DOI 10.1038/nrm2162, PII NRM2162
    • Williams RL, Urbé S. (2007). The emerging shape of the ESCRT machinery. Nat Rev Mol Cell Biol 8:355-68. (Pubitemid 46643239)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 230
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert T, Hurley JH. (2010). Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464:864-9.
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 232
    • 79960897879 scopus 로고    scopus 로고
    • Transforming binding affinities from three dimensions to two with application to cadherin clustering
    • Wu Y, Vendome J, Shapiro L, et al. (2011). Transforming binding affinities from three dimensions to two with application to cadherin clustering. Nature 475:510-13.
    • (2011) Nature , vol.475 , pp. 510-513
    • Wu, Y.1    Vendome, J.2    Shapiro, L.3
  • 233
    • 35548935552 scopus 로고    scopus 로고
    • Structural characterization of the atpase reaction cycle of endosomal AAA protein Vps4
    • DOI 10.1016/j.jmb.2007.09.067, PII S0022283607012661
    • Xiao J, Xia H, Yoshino-Koh K, et al. (2007). Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4. J Mol Biol 374:655-70. (Pubitemid 350018775)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.3 , pp. 655-670
    • Xiao, J.1    Xia, H.2    Yoshino-Koh, K.3    Zhou, J.4    Xu, Z.5
  • 234
    • 37749011364 scopus 로고    scopus 로고
    • Structural basis of Vta1 function in the multivesicular body sorting pathway
    • Xiao J, Xia H, Zhou J, et al. (2008). Structural basis of Vta1 function in the multivesicular body sorting pathway. Dev Cell 14:37-49.
    • (2008) Dev Cell , vol.14 , pp. 37-49
    • Xiao, J.1    Xia, H.2    Zhou, J.3
  • 235
    • 0032539548 scopus 로고    scopus 로고
    • Cell cycle-dependent subcellular localization of the TSG101 protein and mitotic and nuclear abnormalities associated with TSG101 deficiency
    • DOI 10.1073/pnas.95.4.1595
    • Xie W, Li L, Cohen SN. (1998). Cell cycle-dependent subcellular localization of the TSG101 protein and mitotic and nuclear abnormalities associated with TSG101 deficiency. Proc Natl Acad Sci U S A 95:1595-600. (Pubitemid 28103438)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.4 , pp. 1595-1600
    • Xie, W.1    Li, L.2    Cohen, S.N.3
  • 236
    • 0347362792 scopus 로고    scopus 로고
    • Tom1, a VHS domaincontaining protein, interacts with tollip, ubiquitin, and clathrin
    • Yamakami M, Yoshimori T, Yokosawa H. (2003). Tom1, a VHS domaincontaining protein, interacts with tollip, ubiquitin, and clathrin. J Biol Chem 278:52865-72.
    • (2003) J Biol Chem , vol.278 , pp. 52865-52872
    • Yamakami, M.1    Yoshimori, T.2    Yokosawa, H.3
  • 237
    • 49149128470 scopus 로고    scopus 로고
    • Recruitment of Tom1L1/Srcasm to endosomes and the midbody by Tsg101
    • Yanagida-Ishizaki Y, Takei T, Ishizaki R, et al. (2008). Recruitment of Tom1L1/Srcasm to endosomes and the midbody by Tsg101. Cell Struct Funct 33:91-100.
    • (2008) Cell Struct Funct , vol.33 , pp. 91-100
    • Yanagida-Ishizaki, Y.1    Takei, T.2    Ishizaki, R.3
  • 238
    • 77955487325 scopus 로고    scopus 로고
    • Structural role of the Vps4-Vta1 interface in ESCRT-III recycling
    • Yang D, Hurley JH. (2010). Structural role of the Vps4-Vta1 interface in ESCRT-III recycling. Structure 18:976-84.
    • (2010) Structure , vol.18 , pp. 976-984
    • Yang, D.1    Hurley, J.H.2
  • 239
    • 57149085245 scopus 로고    scopus 로고
    • Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
    • Yang D, Rismanchi N, Renvoisé B, et al. (2008). Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B. Nat Struct Mol Biol 15:1278-86.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1278-1286
    • Yang, D.1    Rismanchi, N.2    Renvoisé, B.3
  • 241
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi M, Kondo T, Houghton A, et al. (1999). Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J Biol Chem 274: 31707-12.
    • (1999) J Biol Chem , vol.274 , pp. 31707-31712
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3
  • 242
    • 40049101160 scopus 로고    scopus 로고
    • Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p
    • Yu Z, Gonciarz MD, Sundquist WI, et al. (2008). Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p. J Mol Biol 377: 364-77.
    • (2008) J Mol Biol , vol.377 , pp. 364-377
    • Yu, Z.1    Gonciarz, M.D.2    Sundquist, W.I.3
  • 245
    • 33748334324 scopus 로고    scopus 로고
    • Cep55, a microtubule-bundling protein, associates with centralspindlin to control the midbody integrity and cell abscission during cytokinesis
    • DOI 10.1091/mbc.E06-01-0015
    • Zhao WM, Seki A, Fang G. (2006). Cep55, a microtubule-bundling protein, associates with centralspindlin to control the midbody integrity and cell abscission during cytokinesis. Mol Biol Cell 17: 3881-96. (Pubitemid 44330873)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.9 , pp. 3881-3896
    • Zhao, W.-M.1    Seki, A.2    Fang, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.