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Volumn 205, Issue 1, 2014, Pages 33-49

Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation

Author keywords

[No Author keywords available]

Indexed keywords

ESCRT PROTEIN; PROTEIN; UNCLASSIFIED DRUG; VPS4 PROTEIN;

EID: 84901675911     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201310114     Document Type: Article
Times cited : (142)

References (66)
  • 1
    • 80054079071 scopus 로고    scopus 로고
    • Assembly and disassembly of the ESCRT-III membrane scission complex
    • Adell, M.A., and D. Teis. 2011. Assembly and disassembly of the ESCRT-III membrane scission complex. FEBS Lett. 585:3191-3196. http://dx.doi.org/10.1016/j.febslet.2011.09.001
    • (2011) FEBS Lett , vol.585 , pp. 3191-3196
    • Adell, M.A.1    Teis, D.2
  • 2
    • 33644525938 scopus 로고    scopus 로고
    • Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1
    • Azmi, I., B. Davies, C. Dimaano, J. Payne, D. Eckert, M. Babst, and D.J. Katzmann. 2006. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J. Cell Biol. 172:705-717. http://dx.doi.org/10.1083/jcb.200508166
    • (2006) J. Cell Biol. , vol.172 , pp. 705-717
    • Azmi, I.1    Davies, B.2    Dimaano, C.3    Payne, J.4    Eckert, D.5    Babst, M.6    Katzmann, D.J.7
  • 3
    • 37749048772 scopus 로고    scopus 로고
    • ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1
    • Azmi, I.F., B.A. Davies, J. Xiao, M. Babst, Z. Xu, and D.J. Katzmann. 2008. ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1. Dev. Cell. 14:50-61. http://dx.doi.org/10.1016/j.devcel.2007.10.021
    • (2008) Dev. Cell. , vol.14 , pp. 50-61
    • Azmi, I.F.1    Davies, B.A.2    Xiao, J.3    Babst, M.4    Xu, Z.5    Katzmann, D.J.6
  • 4
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase
    • Babst, M., T.K. Sato, L.M. Banta, and S.D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831. http://dx.doi.org/10.1093/emboj/16.8.1820
    • (1997) Vps4p. EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 5
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., B. Wendland, E.J. Estepa, and S.D. Emr. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993. http://dx.doi.org/10.1093/emboj/17.11.2982
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 6
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst, M., D.J. Katzmann, E.J. Estepa-Sabal, T. Meerloo, and S.D. Emr. 2002a. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell. 3:271-282. http://dx.doi.org/10.1016/S1534-5807(02)00220-4
    • (2002) Dev. Cell. , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 7
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M., D.J. Katzmann, W.B. Snyder, B. Wendland, and S.D. Emr. 2002b. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell. 3:283-289. http://dx.doi.org/10.1016/S1534-5807(02)00219-8
    • (2002) Dev. Cell. , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 10
    • 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., R. Chassefeyre, K. Pernet-Gallay, N. Martinelli, G. Effantin, D.L. Hulsik, A. Belly, Y. Goldberg, C. Chatellard-Causse, B. Blot, 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. 286:40276-40286. http://dx.doi.org/10.1074/jbc.M111.283671
    • (2011) J. Biol. Chem. , vol.286 , pp. 40276-40286
    • Bodon, G.1    Chassefeyre, R.2    Pernet-Gallay, K.3    Martinelli, N.4    Effantin, G.5    Hulsik, D.L.6    Belly, A.7    Goldberg, Y.8    Chatellard-Causse, C.9    Blot, B.10
  • 11
    • 60549104572 scopus 로고    scopus 로고
    • Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion
    • Bonemann, G., A. Pietrosiuk, A. Diemand, H. Zentgraf, and A. Mogk. 2009. Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion. EMBO J. 28:315-325. http://dx.doi.org/ 10.1038/emboj.2008.269
    • (2009) EMBO J , vol.28 , pp. 315-325
    • Bonemann, G.1    Pietrosiuk, A.2    Diemand, A.3    Zentgraf, H.4    Mogk, A.5
  • 12
    • 84886641339 scopus 로고    scopus 로고
    • Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation
    • Buchkovich, N.J., W.M. Henne, S. Tang, and S.D. Emr. 2013. Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation. Dev. Cell. 27:201-214. http://dx.doi.org/10.1016/j.devcel.2013.09.009
    • (2013) Dev. Cell. , vol.27 , pp. 201-214
    • Buchkovich, N.J.1    Henne, W.M.2    Tang, S.3    Emr, S.D.4
  • 13
    • 77958056544 scopus 로고    scopus 로고
    • Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly
    • Davies, B.A., I.F. Azmi, J. Payne, A. Shestakova, B.F. Horazdovsky, M. Babst, and D.J. Katzmann. 2010. Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly. Mol. Biol. Cell. 21:3396-3408. http://dx.doi.org/10.1091/mbc.E10-06-0512
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 3396-3408
    • Davies, B.A.1    Azmi, I.F.2    Payne, J.3    Shestakova, A.4    Horazdovsky, B.F.5    Babst, M.6    Katzmann, D.J.7
  • 14
    • 84872617312 scopus 로고    scopus 로고
    • ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding
    • Effantin, G., A. Dordor, V. Sandrin, N. Martinelli, W.I. Sundquist, G. Schoehn, and W. Weissenhorn. 2013. ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell. Microbiol. 15:213-226. http://dx.doi.org/10.1111/cmi.12041
    • (2013) Cell. Microbiol. , vol.15 , pp. 213-226
    • Effantin, G.1    Dordor, A.2    Sandrin, V.3    Martinelli, N.4    Sundquist, W.I.5    Schoehn, G.6    Weissenhorn, W.7
  • 15
    • 84861167200 scopus 로고    scopus 로고
    • Computational model of cytokinetic abscission driven by ESCRT-III polymerization and remodeling
    • Elia, N., G. Fabrikant, M.M. Kozlov, and J. Lippincott-Schwartz. 2012. Computational model of cytokinetic abscission driven by ESCRT-III polymerization and remodeling. Biophys. J. 102:2309-2320. http://dx.doi.org/10.1016/j.bpj.2012.04.007
    • (2012) Biophys. J. , vol.102 , pp. 2309-2320
    • Elia, N.1    Fabrikant, G.2    Kozlov, M.M.3    Lippincott-Schwartz, J.4
  • 18
    • 58149280810 scopus 로고    scopus 로고
    • In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
    • Falguieres, T., P.P. Luyet, C. Bissig, C.C. Scott, M.C. Velluz, and J. Gruenberg. 2008. In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101. Mol. Biol. Cell. 19:4942-4955. http://dx.doi.org/10.1091/mbc.E08-03-0239
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 4942-4955
    • Falguieres, T.1    Luyet, P.P.2    Bissig, C.3    Scott, C.C.4    Velluz, M.C.5    Gruenberg, J.6
  • 20
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg, J., and H. Stenmark. 2004. The biogenesis of multivesicular endosomes. Nat. Rev. Mol. Cell Biol. 5:317-323. http://dx.doi.org/10.1038/nrm1360
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 22
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • Hanson, P.I., R. Roth, Y. Lin, and J.E. Heuser. 2008. Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J. Cell Biol. 180:389-402. http://dx.doi.org/10.1083/jcb.200707031
    • (2008) J. Cell Biol. , vol.180 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 23
    • 40049105414 scopus 로고    scopus 로고
    • Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p
    • Hartmann, C., M. Chami, U. Zachariae, B.L. de Groot, A. Engel, and M.G. Grutter. 2008. Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p. J. Mol. Biol. 377:352-363. http://dx.doi.org/10.1016/j.jmb.2008.01.010
    • (2008) J. Mol. Biol. , vol.377 , pp. 352-363
    • Hartmann, C.1    Chami, M.2    Zachariae, U.3    de Groot, B.L.4    Engel, A.5    Grutter, M.G.6
  • 24
    • 79960225411 scopus 로고    scopus 로고
    • The ESCRT pathway
    • Henne, W.M., N.J. Buchkovich, and S.D. Emr. 2011. The ESCRT pathway. Dev. Cell. 21:77-91. http://dx.doi.org/10.1016/j.devcel.2011.05.015
    • (2011) Dev. Cell. , vol.21 , pp. 77-91
    • Henne, W.M.1    Buchkovich, N.J.2    Emr, S.D.3
  • 25
    • 84867548612 scopus 로고    scopus 로고
    • The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices
    • Henne, W.M., N.J. Buchkovich, Y. Zhao, and S.D. Emr. 2012. The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices. Cell. 151:356-371. http://dx.doi.org/10.1016/j.cell.2012.08.039
    • (2012) Cell , vol.151 , pp. 356-371
    • Henne, W.M.1    Buchkovich, N.J.2    Zhao, Y.3    Emr, S.D.4
  • 26
    • 33847218215 scopus 로고    scopus 로고
    • Cryopreparation methodology for plant cell biology
    • Hess, M.W. 2007. Cryopreparation methodology for plant cell biology. Methods Cell Biol. 79:57-100. http://dx.doi.org/10.1016/S0091-679X(06)79003-3
    • (2007) Methods Cell Biol , vol.79 , pp. 57-100
    • Hess, M.W.1
  • 27
    • 37849000664 scopus 로고    scopus 로고
    • MIT domainia
    • Hurley, J.H., and D. Yang. 2008. MIT domainia. Dev. Cell. 14:6-8. http://dx.doi.org/10.1016/j.devcel.2007.12.013
    • (2008) Dev. Cell. , vol.14 , pp. 6-8
    • Hurley, J.H.1    Yang, D.2
  • 28
    • 68449095867 scopus 로고    scopus 로고
    • Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis
    • Im, Y.J., T. Wollert, E. Boura, and J.H. Hurley. 2009. Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev. Cell. 17:234-243. http://dx.doi.org/10.1016/j.devcel.2009.07.008
    • (2009) Dev. Cell. , vol.17 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3    Hurley, J.H.4
  • 29
    • 79953296191 scopus 로고    scopus 로고
    • Dynamics of ESCRT protein recruitment during retroviral assembly
    • Jouvenet, N., M. Zhadina, P.D. Bieniasz, and S.M. Simon. 2011. Dynamics of ESCRT protein recruitment during retroviral assembly. Nat. Cell Biol. 13:394-401. http://dx.doi.org/10.1038/ncb2207
    • (2011) Nat. Cell Biol. , vol.13 , pp. 394-401
    • Jouvenet, N.1    Zhadina, M.2    Bieniasz, P.D.3    Simon, S.M.4
  • 30
    • 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
    • Kieffer, C., J.J. Skalicky, E. Morita, I. De Domenico, D.M. Ward, J. Kaplan, and W.I. Sundquist. 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. http://dx.doi.org/10.1016/j.devcel.2008.05.014
    • (2008) Dev. Cell. , vol.15 , 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
  • 31
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., D.N. Mastronarde, and J.R. McIntosh. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71- 76. http://dx.doi.org/10.1006/jsbi.1996.0013
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 32
    • 61449203852 scopus 로고    scopus 로고
    • Three-dimensional structure of AAA ATPase Vps4: advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding
    • Landsberg, M.J., P.R. Vajjhala, R. Rothnagel, A.L. Munn, and B. Hankamer. 2009. Three-dimensional structure of AAA ATPase Vps4: advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding. Structure. 17:427-437. http://dx.doi.org/10.1016/j.str.2008.12.020
    • (2009) Structure , vol.17 , pp. 427-437
    • Landsberg, M.J.1    Vajjhala, P.R.2    Rothnagel, R.3    Munn, A.L.4    Hankamer, B.5
  • 34
    • 0015112403 scopus 로고
    • Hot alcoholic phosphotungstic acid and uranyl acetate as routine stains for thick and thin sections
    • Locke, M., and N. Krishnan. 1971. Hot alcoholic phosphotungstic acid and uranyl acetate as routine stains for thick and thin sections. J. Cell Biol. 50:550- 557. http://dx.doi.org/10.1083/jcb.50.2.550
    • (1971) J. Cell Biol. , vol.50 , pp. 550-557
    • Locke, M.1    Krishnan, N.2
  • 35
    • 73849146092 scopus 로고    scopus 로고
    • The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments
    • Markgraf, D.F., F. Ahnert, H. Arlt, M. Mari, K. Peplowska, N. Epp, J. Griffith, F. Reggiori, and C. Ungermann. 2009. The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments. Mol. Biol. Cell. 20:5276-5289. http://dx.doi.org/10.1091/mbc.E09-06-0521
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 5276-5289
    • Markgraf, D.F.1    Ahnert, F.2    Arlt, H.3    Mari, M.4    Peplowska, K.5    Epp, N.6    Griffith, J.7    Reggiori, F.8    Ungermann, C.9
  • 36
    • 78149276258 scopus 로고    scopus 로고
    • Activation of human VPS4A by ESCRTIII proteins reveals ability of substrates to relieve enzyme autoinhibition
    • Merrill, S.A., and P.I. Hanson. 2010. Activation of human VPS4A by ESCRTIII proteins reveals ability of substrates to relieve enzyme autoinhibition. J. Biol. Chem. 285:35428-35438. http://dx.doi.org/10.1074/jbc.M110.126318
    • (2010) J. Biol. Chem. , vol.285 , pp. 35428-35438
    • Merrill, S.A.1    Hanson, P.I.2
  • 39
    • 33845317263 scopus 로고    scopus 로고
    • Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes
    • Nickerson, D.P., M. West, and G. Odorizzi. 2006. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J. Cell Biol. 175:715-720. http://dx.doi.org/10.1083/jcb.200606113
    • (2006) J. Cell Biol. , vol.175 , pp. 715-720
    • Nickerson, D.P.1    West, M.2    Odorizzi, G.3
  • 40
    • 77949465181 scopus 로고    scopus 로고
    • Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles
    • Nickerson, D.P., M. West, R. Henry, and G. Odorizzi. 2010. Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol. Biol. Cell. 21:1023-1032. http://dx.doi.org/10.1091/mbc.E09-09-0776
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 1023-1032
    • Nickerson, D.P.1    West, M.2    Henry, R.3    Odorizzi, G.4
  • 41
    • 84866295462 scopus 로고    scopus 로고
    • Termination of isoform-selective Vps21/Rab5 signaling at endolysosomal organelles by Msb3/Gyp3
    • Nickerson, D.P., M.R. Russell, S.Y. Lo, H.C. Chapin, J.M. Milnes, and A.J. Merz. 2012. Termination of isoform-selective Vps21/Rab5 signaling at endolysosomal organelles by Msb3/Gyp3. Traffic. 13:1411-1428. http://dx.doi.org/10.1111/j.1600-0854.2012.01390.x
    • (2012) Traffic , vol.13 , pp. 1411-1428
    • Nickerson, D.P.1    Russell, M.R.2    Lo, S.Y.3    Chapin, H.C.4    Milnes, J.M.5    Merz, A.J.6
  • 42
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • Obita, T., S. Saksena, S. Ghazi-Tabatabai, D.J. Gill, O. Perisic, S.D. Emr, and R.L. Williams. 2007. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature. 449:735-739. http://dx.doi.org/10.1038/nature06171
    • (2007) Nature , vol.449 , 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
  • 43
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi, G., M. Babst, and S.D. Emr. 1998. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell. 95:847-858. http://dx.doi.org/10.1016/S0092-8674(00)81707-9
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 44
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa, M., D.E. Anderson, and H.P. Erickson. 2008. Reconstitution of contractile FtsZ rings in liposomes. Science. 320:792-794. http://dx.doi.org/10.1126/science.1154520
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 45
    • 80051924474 scopus 로고    scopus 로고
    • Molecular basis for the unique role of the AAA+ chaperone ClpV in type VI protein secretion
    • Pietrosiuk, A., E.D. Lenherr, S. Falk, G. Bonemann, J. Kopp, H. Zentgraf, I. Sinning, and A. Mogk. 2011. Molecular basis for the unique role of the AAA+ chaperone ClpV in type VI protein secretion. J. Biol. Chem. 286:30010-30021. http://dx.doi.org/10.1074/jbc.M111.253377
    • (2011) J. Biol. Chem. , vol.286 , pp. 30010-30021
    • Pietrosiuk, A.1    Lenherr, E.D.2    Falk, S.3    Bonemann, G.4    Kopp, J.5    Zentgraf, H.6    Sinning, I.7    Mogk, A.8
  • 46
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C., and H. Stenmark. 2009. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature. 458:445-452. http://dx.doi.org/10.1038/nature07961
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 47
    • 84877986315 scopus 로고    scopus 로고
    • Doa4 function in ILV budding is restricted through its interaction with the Vps20 subunit of ESCRT-III
    • Richter, C.M., M. West, and G. Odorizzi. 2013. Doa4 function in ILV budding is restricted through its interaction with the Vps20 subunit of ESCRT-III. J. Cell Sci. 126:1881-1890. http://dx.doi.org/10.1242/jcs.122499
    • (2013) J. Cell Sci. , vol.126 , pp. 1881-1890
    • Richter, C.M.1    West, M.2    Odorizzi, G.3
  • 48
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak, A., and R.D. Vale. 2008. Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature. 451:363-367. http://dx.doi.org/10.1038/nature06482
    • (2008) Nature , vol.451 , pp. 363-367
    • Roll-Mecak, A.1    Vale, R.D.2
  • 49
    • 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, M.R., T. Shideler, D.P. Nickerson, M. West, and G. Odorizzi. 2012. Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase. J. Cell Sci. 125:5208- 5220. http://dx.doi.org/10.1242/jcs.111310
    • (2012) J. Cell Sci. , vol.125 , pp. 5208-5220
    • Russell, M.R.1    Shideler, T.2    Nickerson, D.P.3    West, M.4    Odorizzi, G.5
  • 50
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • Saksena, S., J. Wahlman, D. Teis, A.E. Johnson, and S.D. Emr. 2009. Functional reconstitution of ESCRT-III assembly and disassembly. Cell. 136:97-109. http://dx.doi.org/10.1016/j.cell.2008.11.013
    • (2009) Cell , vol.136 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 51
    • 84857309195 scopus 로고    scopus 로고
    • The ESCRT machinery
    • Schmidt, O., and D. Teis. 2012. The ESCRT machinery. Curr. Biol. 22:R116- R120. http://dx.doi.org/10.1016/j.cub.2012.01.028
    • (2012) Curr. Biol. , vol.22
    • Schmidt, O.1    Teis, D.2
  • 54
    • 84884185317 scopus 로고    scopus 로고
    • The linker region plays a regulatory role in assembly and activity of the Vps4 AAA ATPase
    • Shestakova, A., M. Curtiss, B.A. Davies, D.J. Katzmann, and M. Babst. 2013. The linker region plays a regulatory role in assembly and activity of the Vps4 AAA ATPase. J. Biol. Chem. 288:26810-26819. http://dx.doi.org/10.1074/jbc.M113.497032
    • (2013) J. Biol. Chem. , vol.288 , pp. 26810-26819
    • Shestakova, A.1    Curtiss, M.2    Davies, B.A.3    Katzmann, D.J.4    Babst, M.5
  • 57
    • 53249131094 scopus 로고    scopus 로고
    • Ordered assembly of the ESCRTIII complex on endosomes is required to sequester cargo during MVB formation
    • Teis, D., S. Saksena, and S.D. Emr. 2008. Ordered assembly of the ESCRTIII complex on endosomes is required to sequester cargo during MVB formation. Dev. Cell. 15:578-589. http://dx.doi.org/10.1016/j.devcel.2008.08.013
    • (2008) Dev. Cell. , vol.15 , pp. 578-589
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 58
    • 77649335931 scopus 로고    scopus 로고
    • ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation
    • Teis, D., S. Saksena, B.L. Judson, and S.D. Emr. 2010. ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation. EMBO J. 29:871-883. http://dx.doi.org/10.1038/emboj.2009.408
    • (2010) EMBO J , vol.29 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3    Emr, S.D.4
  • 60
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and S.D. Emr. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792. http://dx.doi.org/10.1083/jcb.128.5.779
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 61
    • 78951470141 scopus 로고    scopus 로고
    • Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast
    • Wemmer, M., I. Azmi, M. West, B. Davies, D. Katzmann, and G. Odorizzi. 2011. Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast. J. Cell Biol. 192:295-306. http://dx.doi.org/10.1083/jcb.201007018
    • (2011) J. Cell Biol. , vol.192 , pp. 295-306
    • Wemmer, M.1    Azmi, I.2    West, M.3    Davies, B.4    Katzmann, D.5    Odorizzi, G.6
  • 62
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert, T., and J.H. Hurley. 2010. Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature. 464:864-869. http://dx.doi.org/10.1038/nature08849
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 63
    • 62249210955 scopus 로고    scopus 로고
    • Membrane scission by the ESCRT-III complex
    • Wollert, T., C. Wunder, J. Lippincott-Schwartz, and J.H. Hurley. 2009. Membrane scission by the ESCRT-III complex. Nature. 458:172-177. http://dx.doi.org/10.1038/nature07836
    • (2009) Nature , vol.458 , pp. 172-177
    • Wollert, T.1    Wunder, C.2    Lippincott-Schwartz, J.3    Hurley, J.H.4
  • 64
    • 68149094429 scopus 로고    scopus 로고
    • Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis
    • Xiao, J., X.W. Chen, B.A. Davies, A.R. Saltiel, D.J. Katzmann, and Z. Xu. 2009. Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis. Mol. Biol. Cell. 20:3514-3524. http://dx.doi.org/10.1091/mbc.E09-05-0403
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 3514-3524
    • Xiao, J.1    Chen, X.W.2    Davies, B.A.3    Saltiel, A.R.4    Katzmann, D.J.5    Xu, Z.6
  • 65
    • 40049101160 scopus 로고    scopus 로고
    • Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p
    • Yu, Z., M.D. Gonciarz, W.I. Sundquist, C.P. Hill, and G.J. Jensen. 2008. Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p. J. Mol. Biol. 377:364-377. http://dx.doi.org/10.1016/j.jmb.2008.01.009
    • (2008) J. Mol. Biol. , vol.377 , pp. 364-377
    • Yu, Z.1    Gonciarz, M.D.2    Sundquist, W.I.3    Hill, C.P.4    Jensen, G.J.5
  • 66
    • 34247396927 scopus 로고    scopus 로고
    • Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding
    • Zamborlini, A., Y. Usami, S.R. Radoshitzky, E. Popova, G. Palu, and H. Gottlinger. 2006. Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding. Proc. Natl. Acad. Sci. USA. 103:19140-19145. http://dx.doi.org/10.1073/pnas.0603788103
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 19140-19145
    • Zamborlini, A.1    Usami, Y.2    Radoshitzky, S.R.3    Popova, E.4    Palu, G.5    Gottlinger, H.6


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