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Volumn , Issue , 2016, Pages 3288-3302

ESCRT-III and Vps4: a dynamic multipurpose tool for membrane budding and scission

Author keywords

adaptors; ESCRT III; membrane remodelling; Vps4 AAA ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ESCRT III PROTEIN; ESCRT PROTEIN; PROTEIN VPS4; UNCLASSIFIED DRUG;

EID: 84987981735     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13688     Document Type: Article
Times cited : (90)

References (147)
  • 1
    • 47149100894 scopus 로고    scopus 로고
    • Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage
    • Leung KF, Dacks JB & Field MC (2008) Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage. Traffic 9, 1698–1716.
    • (2008) Traffic , vol.9 , pp. 1698-1716
    • Leung, K.F.1    Dacks, J.B.2    Field, M.C.3
  • 4
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • Samson R, Obita T, Freund S, Williams R & Bell S (2008) A role for the ESCRT system in cell division in archaea. Science 322, 1710–1713.
    • (2008) Science , vol.322 , pp. 1710-1713
    • Samson, R.1    Obita, T.2    Freund, S.3    Williams, R.4    Bell, S.5
  • 6
    • 84856768251 scopus 로고    scopus 로고
    • Regulation of membrane protein degradation by starvation-response pathways
    • Jones CB, Ott EM, Keener JM, Curtiss M, Sandrin V & Babst M (2012) Regulation of membrane protein degradation by starvation-response pathways. Traffic 13, 468–482.
    • (2012) Traffic , vol.13 , pp. 468-482
    • Jones, C.B.1    Ott, E.M.2    Keener, J.M.3    Curtiss, M.4    Sandrin, V.5    Babst, M.6
  • 7
    • 84942826638 scopus 로고    scopus 로고
    • Starvation-dependent regulation of golgi quality control links the TOR signaling and vacuolar protein sorting pathways
    • Dobzinski N, Chuartzman SG, Kama R, Schuldiner M & Gerst JE (2015) Starvation-dependent regulation of golgi quality control links the TOR signaling and vacuolar protein sorting pathways. Cell Rep 12, 1876–1886.
    • (2015) Cell Rep , vol.12 , pp. 1876-1886
    • Dobzinski, N.1    Chuartzman, S.G.2    Kama, R.3    Schuldiner, M.4    Gerst, J.E.5
  • 8
    • 84941773739 scopus 로고    scopus 로고
    • ESCRTs cooperate with a selective autophagy receptor to mediate vacuolar targeting of soluble cargos
    • Liu XM, Sun LL, Hu W, Ding YH, Dong MQ & Du LL (2015) ESCRTs cooperate with a selective autophagy receptor to mediate vacuolar targeting of soluble cargos. Mol Cell 59, 1035–1042.
    • (2015) Mol Cell , vol.59 , pp. 1035-1042
    • Liu, X.M.1    Sun, L.L.2    Hu, W.3    Ding, Y.H.4    Dong, M.Q.5    Du, L.L.6
  • 12
    • 84901766763 scopus 로고    scopus 로고
    • The role of the endosomal sorting complexes required for transport (ESCRT) in tumorigenesis
    • Mattissek C & Teis D (2014) The role of the endosomal sorting complexes required for transport (ESCRT) in tumorigenesis. Mol Membr Biol 31, 111–119.
    • (2014) Mol Membr Biol , vol.31 , pp. 111-119
    • Mattissek, C.1    Teis, D.2
  • 13
    • 59749096466 scopus 로고    scopus 로고
    • ESCRTs and human disease
    • Saksena S & Emr SD (2009) ESCRTs and human disease. Biochem Soc Trans 37, 167–172.
    • (2009) Biochem Soc Trans , vol.37 , pp. 167-172
    • Saksena, S.1    Emr, S.D.2
  • 14
    • 67349135343 scopus 로고    scopus 로고
    • ESCRT proteins in physiology and disease
    • Stuffers S, Brech A & Stenmark H (2009) ESCRT proteins in physiology and disease. Exp Cell Res 315, 1619–1626.
    • (2009) Exp Cell Res , vol.315 , pp. 1619-1626
    • Stuffers, S.1    Brech, A.2    Stenmark, H.3
  • 16
    • 84859630113 scopus 로고    scopus 로고
    • ESCRT-III governs the aurora B-mediated abscission checkpoint through CHMP4C
    • Carlton JG, Caballe A, Agromayor M, Kloc M & Martin-Serrano J (2012) ESCRT-III governs the aurora B-mediated abscission checkpoint through CHMP4C. Science 336, 220–225.
    • (2012) Science , vol.336 , pp. 220-225
    • Carlton, J.G.1    Caballe, A.2    Agromayor, M.3    Kloc, M.4    Martin-Serrano, J.5
  • 17
    • 79956277415 scopus 로고    scopus 로고
    • Frontotemporal Dementia Caused by CHMP2B Mutations
    • Isaacs AM, Johannsen P, Holm I & Nielsen JE & Consortium, F. R. E. J. A. (2011) Frontotemporal Dementia Caused by CHMP2B Mutations. Curr Alzheimer Res 8, 246–251.
    • (2011) Curr Alzheimer Res , vol.8 , pp. 246-251
    • Isaacs, A.M.1    Johannsen, P.2    Holm, I.3    Nielsen, J.E.4
  • 19
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee JA, Beigneux A, Ahmad ST, Young SG & Gao FB (2007) ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Current Biol 17, 1561–1567.
    • (2007) Current Biol , vol.17 , pp. 1561-1567
    • Lee, J.A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.B.5
  • 23
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T & Emr SD (2002) Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 3, 271–282.
    • (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
  • 25
    • 33845317263 scopus 로고    scopus 로고
    • Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes
    • Nickerson DP, West M & Odorizzi G (2006) Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J Cell Biol 175, 715–720.
    • (2006) J Cell Biol , vol.175 , pp. 715-720
    • Nickerson, D.P.1    West, M.2    Odorizzi, G.3
  • 31
    • 78951470141 scopus 로고    scopus 로고
    • Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast
    • Wemmer M, Azmi I, West M, Davies B, Katzmann D & Odorizzi G (2011) Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast. J Cell Biol 192, 295–306.
    • (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
  • 33
    • 34447527768 scopus 로고    scopus 로고
    • Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain
    • 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, 1068–1079.
    • (2007) Traffic , vol.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 35
    • 17144377439 scopus 로고    scopus 로고
    • Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting
    • Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y & Maki M (2005) Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting. Biochem J 387, 17–26.
    • (2005) Biochem J , vol.387 , pp. 17-26
    • Yorikawa, C.1    Shibata, H.2    Waguri, S.3    Hatta, K.4    Horii, M.5    Katoh, K.6    Kobayashi, T.7    Uchiyama, Y.8    Maki, M.9
  • 36
    • 84886641339 scopus 로고    scopus 로고
    • Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation
    • Buchkovich NJ, Henne WM, Shaogeng T & Emr SD (2013) Essential N-terminal insertion motif anchors the ESCRT-III filament during MVB vesicle formation. Dev Cell 27, 201–214.
    • (2013) Dev Cell , vol.27 , pp. 201-214
    • Buchkovich, N.J.1    Henne, W.M.2    Shaogeng, T.3    Emr, S.D.4
  • 38
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • 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, 2982–2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 40
    • 35548935552 scopus 로고    scopus 로고
    • Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4
    • Xiao J, Xia H, Yoshino-Koh K, Zhou J & Xu Z (2007) Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4. J Mol Biol 374, 655–670.
    • (2007) J Mol Biol , vol.374 , pp. 655-670
    • Xiao, J.1    Xia, H.2    Yoshino-Koh, K.3    Zhou, J.4    Xu, Z.5
  • 45
    • 84876903053 scopus 로고    scopus 로고
    • Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine
    • Stinson BM, Nager AR, Glynn SE, Schmitz KR, Baker TA & Sauer RT (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153, 628–639.
    • (2013) Cell , vol.153 , pp. 628-639
    • Stinson, B.M.1    Nager, A.R.2    Glynn, S.E.3    Schmitz, K.R.4    Baker, T.A.5    Sauer, R.T.6
  • 46
    • 40049101160 scopus 로고    scopus 로고
    • Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p
    • Yu Z, Gonciarz MD, Sundquist WI, Hill CP & Jensen GJ (2008) Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p. J Mol Biol 377, 364–377.
    • (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
  • 47
    • 84901675911 scopus 로고    scopus 로고
    • Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation
    • Adell MA, Vogel GF, Pakdel M, Muller M, Lindner H, Hess MW & Teis D (2014) Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation. J Cell Biol 205, 33–49.
    • (2014) J Cell Biol , vol.205 , pp. 33-49
    • Adell, M.A.1    Vogel, G.F.2    Pakdel, M.3    Muller, M.4    Lindner, H.5    Hess, M.W.6    Teis, D.7
  • 49
    • 84949663759 scopus 로고    scopus 로고
    • Conformational changes in the endosomal sorting complex required for transport-III subunit Ist1 lead to distinct modes of ATPase Vps4 regulation
    • Tan J, Davies BA, Payne JA, Benson LM & Katzmann DJ (2015) Conformational changes in the endosomal sorting complex required for transport-III subunit Ist1 lead to distinct modes of ATPase Vps4 regulation. J Biol Chem M115, 665604.
    • (2015) J Biol Chem , vol.M115 , pp. 665604
    • Tan, J.1    Davies, B.A.2    Payne, J.A.3    Benson, L.M.4    Katzmann, D.J.5
  • 50
    • 84871605394 scopus 로고    scopus 로고
    • Structural basis of molecular recognition between ESCRT-III like protein Vps60 and AAA-ATPase regulator Vta1 in the multi-vesicular body pathway
    • Zhongzheng Y, Cody V, Jiaying J, Xu Z, Jianping L, Jie S, Bin Z, Wenxian L, Fuchung G, Maili L et al. (2012) Structural basis of molecular recognition between ESCRT-III like protein Vps60 and AAA-ATPase regulator Vta1 in the multi-vesicular body pathway. J Biol Chem 287, 43899–43908.
    • (2012) J Biol Chem , vol.287 , pp. 43899-43908
    • Zhongzheng, Y.1    Cody, V.2    Jiaying, J.3    Xu, Z.4    Jianping, L.5    Jie, S.6    Bin, Z.7    Wenxian, L.8    Fuchung, G.9    Maili, L.10
  • 51
    • 84930413153 scopus 로고    scopus 로고
    • Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation
    • Yang B, Stjepanovic G, Shen Q, Martin A & Hurley JH (2015) Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation. Nat Struct Mol Biol 22, 492–498.
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 492-498
    • Yang, B.1    Stjepanovic, G.2    Shen, Q.3    Martin, A.4    Hurley, J.H.5
  • 52
    • 0000272957 scopus 로고
    • Isolation of yeast mutants defective in protein targeting to the vacuole
    • Bankaitis VA, Johnson LM & Emr SD (1986) Isolation of yeast mutants defective in protein targeting to the vacuole. Proc Natl Acad Sci USA 83, 9075–9079.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9075-9079
    • Bankaitis, V.A.1    Johnson, L.M.2    Emr, S.D.3
  • 53
    • 0022898326 scopus 로고
    • Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • Rothman JH & Stevens TH (1986) Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell 47, 1041–1051.
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 54
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson JS, Klionsky DJ, Banta LM & Emr SD (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8, 4936–4948.
    • (1988) Mol Cell Biol , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 55
    • 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, 1389–1402.
    • (1992) Mol Biol Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 56
    • 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
    • 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, 145–155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 57
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann DJ, Stefan CJ, Babst M & Emr SD (2003) Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 162, 413–423.
    • (2003) J Cell Biol , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 58
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst M, Sato TK, Banta LM & Emr SD (1997) Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J 16, 1820–1831.
    • (1997) EMBO J , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 59
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst M, Katzmann DJ, Snyder WB, Wendland B & Emr SD (2002) Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 3, 283–289.
    • (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
  • 60
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • Bilodeau PS, Winistorfer SC, Kearney WR, Robertson AD & Piper RC (2003) Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J Cell Biol 163, 237–243.
    • (2003) J Cell Biol , vol.163 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 62
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M (2005) A protein's final ESCRT. Traffic 6, 2–9.
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 63
    • 84898616566 scopus 로고    scopus 로고
    • Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity
    • Vlid CJ & Xu Z (2014) Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity. J Biol Chem 289, 10378–10386.
    • (2014) J Biol Chem , vol.289 , pp. 10378-10386
    • Vlid, C.J.1    Xu, Z.2
  • 65
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi G, Babst M & Emr SD (1998) Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 95, 847–858.
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 66
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann DJ, Odorizzi G & Emr SD (2002) Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 3, 893–905.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 67
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper RC & Katzmann DJ (2007) Biogenesis and function of multivesicular bodies. Annu Rev Cell Dev Biol 23, 519–547.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 68
    • 84857309195 scopus 로고    scopus 로고
    • The ESCRT machinery
    • Schmidt O & Teis D (2012) The ESCRT machinery. Curr Biol 22, R116–R120.
    • (2012) Curr Biol , vol.22 , pp. R116-R120
    • Schmidt, O.1    Teis, D.2
  • 69
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams RL & Urbe S (2007) The emerging shape of the ESCRT machinery. Nat Rev Mol Cell Biol 8, 355–368.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 70
    • 84921828412 scopus 로고    scopus 로고
    • Constitutively active ESCRT-II suppresses the MVB-sorting phenotype of ESCRT-0 and ESCRT-I mutants
    • Mageswaran SK, Johnson NK, Odorizzi G & Babst M (2015) Constitutively active ESCRT-II suppresses the MVB-sorting phenotype of ESCRT-0 and ESCRT-I mutants. Mol Biol Cell 26, 554–568.
    • (2015) Mol Biol Cell , vol.26 , pp. 554-568
    • Mageswaran, S.K.1    Johnson, N.K.2    Odorizzi, G.3    Babst, M.4
  • 73
    • 5044245523 scopus 로고    scopus 로고
    • ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes
    • Teo H, Perisic O, Gonzalez 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, 559–569.
    • (2004) Dev Cell , vol.7 , pp. 559-569
    • Teo, H.1    Perisic, O.2    Gonzalez, B.3    Williams, R.L.4
  • 74
    • 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 B & Emr S (2010) ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation. EMBO J 29 (5), 871–883.
    • (2010) EMBO J , vol.29 , Issue.5 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.3    Emr, S.4
  • 75
    • 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, 234–243.
    • (2009) Dev Cell , vol.17 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3    Hurley, J.H.4
  • 76
    • 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, 578–589.
    • (2008) Dev Cell , vol.15 , pp. 578-589
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 77
    • 81055157988 scopus 로고    scopus 로고
    • Exosome secretion: molecular mechanisms and roles in immune responses
    • Bobrie A, Colombo M, Raposo G & Thery C (2011) Exosome secretion: molecular mechanisms and roles in immune responses. Traffic 12, 1659–1668.
    • (2011) Traffic , vol.12 , pp. 1659-1668
    • Bobrie, A.1    Colombo, M.2    Raposo, G.3    Thery, C.4
  • 78
    • 79960096964 scopus 로고    scopus 로고
    • Exosomes: secreted vesicles and intercellular communications
    • Thery C (2011) Exosomes: secreted vesicles and intercellular communications. F1000 Biol Rep 3, 15. doi: 10.3410/B3-15.
    • (2011) F1000 Biol Rep , vol.3 , pp. 15
    • Thery, C.1
  • 80
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles
    • Thery C, Broussac M, Veron P, Ricciardi-Castagnoli P & Raposo G (2001) Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles. J Immunol 166, 7309–7318.
    • (2001) J Immunol , vol.166 , pp. 7309-7318
    • Thery, C.1    Broussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5
  • 81
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: a compendium of exosomal proteins and RNA
    • Mathivanan S & Simpson RJ (2009) ExoCarta: a compendium of exosomal proteins and RNA. Proteomics 9, 4997–5000.
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 82
    • 84858230240 scopus 로고    scopus 로고
    • Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein
    • Nabhan JF, Hu R, Oh RS, Cohen SN & Lu Q (2012) Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein. Proc Natl Acad Sci USA 109, 4146–4151.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4146-4151
    • Nabhan, J.F.1    Hu, R.2    Oh, R.S.3    Cohen, S.N.4    Lu, Q.5
  • 84
    • 84890458696 scopus 로고    scopus 로고
    • Analysis of ESCRT functions in exosomes biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles
    • Colombo M, Moita C, van Niel G, Kowal J, Vigneron J, Benaroch P, Manel N, Moita LF, Thery C & Raposo G (2013) Analysis of ESCRT functions in exosomes biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles. J Cell Sci 126, 5553–5565.
    • (2013) J Cell Sci , vol.126 , pp. 5553-5565
    • Colombo, M.1    Moita, C.2    van Niel, G.3    Kowal, J.4    Vigneron, J.5    Benaroch, P.6    Manel, N.7    Moita, L.F.8    Thery, C.9    Raposo, G.10
  • 85
    • 1642408871 scopus 로고    scopus 로고
    • Degradation of AP2 during reticulocyte maturation enhances binding of hsc70 and Alix to a common site on TFR for sorting into exosomes
    • Géminard C, De Gassart A, Blanc L & Vidal M (2004) Degradation of AP2 during reticulocyte maturation enhances binding of hsc70 and Alix to a common site on TFR for sorting into exosomes. Traffic 5, 181–193.
    • (2004) Traffic , vol.5 , pp. 181-193
    • Géminard, C.1    De Gassart, A.2    Blanc, L.3    Vidal, M.4
  • 88
    • 84926524813 scopus 로고    scopus 로고
    • Heparanase activates the syndecan-syntenin-ALIX exosome pathway
    • Roucourt B, Meeussen S, Bao J, Zimmermann P & David G (2015) Heparanase activates the syndecan-syntenin-ALIX exosome pathway. Cell Res 25, 412–428.
    • (2015) Cell Res , vol.25 , pp. 412-428
    • Roucourt, B.1    Meeussen, S.2    Bao, J.3    Zimmermann, P.4    David, G.5
  • 90
    • 82955227444 scopus 로고    scopus 로고
    • The P4-ATPase TAT-5 inhibits the budding of extracellular vesicles in C. elegans embryos
    • Wehman AM, Poggioli C, Schweinsberg P, Grant BD & Nance J (2011) The P4-ATPase TAT-5 inhibits the budding of extracellular vesicles in C. elegans embryos. Curr Biol 21, 1951–1959.
    • (2011) Curr Biol , vol.21 , pp. 1951-1959
    • Wehman, A.M.1    Poggioli, C.2    Schweinsberg, P.3    Grant, B.D.4    Nance, J.5
  • 91
    • 79959211941 scopus 로고    scopus 로고
    • Host factors involved in retroviral budding and release
    • Martin-Serrano J & Neil SJ (2011) Host factors involved in retroviral budding and release. Nat Rev Microbiol 9, 519–531.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 519-531
    • Martin-Serrano, J.1    Neil, S.J.2
  • 95
    • 12144258074 scopus 로고    scopus 로고
    • HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway
    • Martin-Serrano J, Eastman SW, Chung W & Bieniasz PD (2005) HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway. J Cell Biol 168, 89–101.
    • (2005) J Cell Biol , vol.168 , pp. 89-101
    • Martin-Serrano, J.1    Eastman, S.W.2    Chung, W.3    Bieniasz, P.D.4
  • 96
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B, Calistri A, Craig S, Popova E & Gottlinger HG (2003) AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114, 689–699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 98
    • 84872617312 scopus 로고    scopus 로고
    • ESCRT CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding
    • Effantin G, Dordor A, Sandrin V, Martinelli C & Sundquist W (2013) ESCRT CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell Microbiol 15, 213–226.
    • (2013) Cell Microbiol , vol.15 , pp. 213-226
    • Effantin, G.1    Dordor, A.2    Sandrin, V.3    Martinelli, C.4    Sundquist, W.5
  • 99
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs JA, Wilk T, Welker R, Krausslich HG & Fuller SD (2003) Structural organization of authentic, mature HIV-1 virions and cores. EMBO J 22, 1707–1715.
    • (2003) EMBO J , vol.22 , pp. 1707-1715
    • Briggs, J.A.1    Wilk, T.2    Welker, R.3    Krausslich, H.G.4    Fuller, S.D.5
  • 100
    • 84988547064 scopus 로고    scopus 로고
    • Structure of cellular ESCRT-III spirals and their relationship to HIV budding
    • Cashikar AG, Shim S, Roth R, Maldazys MR, Heuser JE & Hanson PI (2014) Structure of cellular ESCRT-III spirals and their relationship to HIV budding. eLife 3, e02184. doi: 10.7554/eLife.02184.
    • (2014) eLife , vol.3
    • Cashikar, A.G.1    Shim, S.2    Roth, R.3    Maldazys, M.R.4    Heuser, J.E.5    Hanson, P.I.6
  • 104
    • 79953296191 scopus 로고    scopus 로고
    • Dynamics of ESCRT protein recruitment during retroviral assembly
    • Jouvenet N, Zhadina M, Bieniasz P & Simon S (2011) Dynamics of ESCRT protein recruitment during retroviral assembly. Nat Cell Biol 13, 394–401.
    • (2011) Nat Cell Biol , vol.13 , pp. 394-401
    • Jouvenet, N.1    Zhadina, M.2    Bieniasz, P.3    Simon, S.4
  • 106
    • 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, 201–214.
    • (2013) Dev Cell , vol.27 , pp. 201-214
    • Buchkovich, N.J.1    Henne, W.M.2    Tang, S.3    Emr, S.D.4
  • 107
    • 84952690378 scopus 로고    scopus 로고
    • Negative membrane curvature catalyzes nucleation of endosomal sorting complex required for transport (ESCRT)-III assembly
    • Lee IH, Kai H, Carlson LA, Groves JT & Hurley JH (2015) Negative membrane curvature catalyzes nucleation of endosomal sorting complex required for transport (ESCRT)-III assembly. Proc Natl Acad Sci USA 112, 15892–15897.
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. 15892-15897
    • Lee, I.H.1    Kai, H.2    Carlson, L.A.3    Groves, J.T.4    Hurley, J.H.5
  • 108
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery
    • Carlton JG & Martin-Serrano J (2007) Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316, 1908–1912.
    • (2007) Science , vol.316 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 109
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK & Sundquist WI (2007) Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J 26, 4215–4227.
    • (2007) EMBO J , vol.26 , 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
  • 110
    • 54949088988 scopus 로고    scopus 로고
    • Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55
    • Lee HH, Elia N, Ghirlando R, Lippincott-Schwartz J & Hurley JH (2008) Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science 322, 576–580.
    • (2008) Science , vol.322 , pp. 576-580
    • Lee, H.H.1    Elia, N.2    Ghirlando, R.3    Lippincott-Schwartz, J.4    Hurley, J.H.5
  • 112
    • 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 USA 105, 10541–10546.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10541-10546
    • Carlton, J.G.1    Agromayor, M.2    Martin-Serrano, J.3
  • 116
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • Reid E, Connell J, Edwards TL, Duley S, Brown SE & Sanderson CM (2005) The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum Mol Genet 14, 19–38.
    • (2005) Hum Mol Genet , vol.14 , pp. 19-38
    • Reid, E.1    Connell, J.2    Edwards, T.L.3    Duley, S.4    Brown, S.E.5    Sanderson, C.M.6
  • 117
    • 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 T, Hurley J & Lippincott-Schwartz J (2011) Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission. PNAS 108, 4846–4851.
    • (2011) PNAS , vol.108 , pp. 4846-4851
    • Elia, N.1    Sougrat, R.2    Spurlin, T.3    Hurley, J.4    Lippincott-Schwartz, J.5
  • 118
    • 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, 2309–2320.
    • (2012) Biophys J , vol.102 , pp. 2309-2320
    • Elia, N.1    Fabrikant, G.2    Kozlov, M.M.3    Lippincott-Schwartz, J.4
  • 120
    • 84864212914 scopus 로고    scopus 로고
    • The chromosomal passenger complex controls the function of endosomal sorting complex required for transport-III Snf7 proteins during cytokinesis
    • Capalbo L, Montembault E, Takeda T, Bassi ZI, Glover DM & D'Avino PP (2012) The chromosomal passenger complex controls the function of endosomal sorting complex required for transport-III Snf7 proteins during cytokinesis. Open Biol 2, 120070.
    • (2012) Open Biol , vol.2 , pp. 120070
    • Capalbo, L.1    Montembault, E.2    Takeda, T.3    Bassi, Z.I.4    Glover, D.M.5    D'Avino, P.P.6
  • 121
    • 84907322903 scopus 로고    scopus 로고
    • Endocytic pathways downregulate the L1-type cell adhesion molecule neuroglian to promote dendrite pruning in Drosophila
    • Zhang H, Wang Y, Wong JJ, Lim KL, Liou YC, Wang H & Yu F (2014) Endocytic pathways downregulate the L1-type cell adhesion molecule neuroglian to promote dendrite pruning in Drosophila. Dev Cell 30, 463–478.
    • (2014) Dev Cell , vol.30 , pp. 463-478
    • Zhang, H.1    Wang, Y.2    Wong, J.J.3    Lim, K.L.4    Liou, Y.C.5    Wang, H.6    Yu, F.7
  • 128
    • 84916928432 scopus 로고    scopus 로고
    • Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4
    • Webster BM, Colombi P, Jäger J & Lusk CP (2014) Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4. Cell 159, 388–401.
    • (2014) Cell , vol.159 , pp. 388-401
    • Webster, B.M.1    Colombi, P.2    Jäger, J.3    Lusk, C.P.4
  • 129
  • 130
  • 131
    • 70350322311 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression
    • Pawliczek T & Crump CM (2009) Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 83, 11254–11264.
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 132
    • 85051910021 scopus 로고    scopus 로고
    • Evidence for a non-endosomal Function of the Saccharomyces cerevisiae ESCRT-III Like Protein Chm7
    • Bauer I, Brune T, Preiss R & Köllinger R (2015) Evidence for a non-endosomal Function of the Saccharomyces cerevisiae ESCRT-III Like Protein Chm7. Genetics 115, 178939.
    • (2015) Genetics , vol.115 , pp. 178939
    • Bauer, I.1    Brune, T.2    Preiss, R.3    Köllinger, R.4
  • 134
    • 84934974992 scopus 로고    scopus 로고
    • The VPS-20 subunit of the endosomal sorting complex ESCRT-III exhibits an open conformation in the absence of upstream activation
    • Schuh AL, Hanna M, Quinney K, Wang L, Sarkeshik A, Yates JR 3rd & Audhya A (2015) The VPS-20 subunit of the endosomal sorting complex ESCRT-III exhibits an open conformation in the absence of upstream activation. Biochem J 466, 625–637.
    • (2015) Biochem J , vol.466 , pp. 625-637
    • Schuh, A.L.1    Hanna, M.2    Quinney, K.3    Wang, L.4    Sarkeshik, A.5    Yates, J.R.6    Audhya, A.7
  • 135
    • 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, 871–883.
    • (2010) EMBO J , vol.29 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3    Emr, S.D.4
  • 137
    • 84867548612 scopus 로고    scopus 로고
    • The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices
    • Henne WM, Buchkovich NJ, Yingying Z & Emr SD (2012) The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices. Cell 151, 356–371.
    • (2012) Cell , vol.151 , pp. 356-371
    • Henne, W.M.1    Buchkovich, N.J.2    Yingying, Z.3    Emr, S.D.4
  • 140
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • Saksena S, Wahlman J, Teis D, Johnson AE & Emr SD (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    Johnson, A.E.4    Emr, S.D.5
  • 144
    • 58149280810 scopus 로고    scopus 로고
    • In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
    • Falguieres T, Luyet PP, Bissig C, Scott CC, Velluz MC & Gruenberg J (2008) In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101. Mol Biol Cell 19, 4942–4955.
    • (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
  • 145
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • 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.
    • (2008) J Cell Biol , vol.180 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 146
    • 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, Martinelli N, Effantin G, Hulsik DL, Belly A, Goldberg Y, Chatellard-Causse C, Blot B 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.
    • (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


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