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Volumn 6, Issue 10, 2011, Pages 1159-1170

Essential and supporting host cell factors for HIV-1 budding

Author keywords

budding; CHMP2; CHMP3; CHMP4; CHMP6; ESCRT I; ESCRT III; Gag; HIV 1; L domain; membrane fission; VPS4

Indexed keywords

ADAPTOR PROTEIN; ALIX PROTEIN; CALMODULIN; CHMP2 PROTEIN; CHMP3 PROTEIN; CHMP4 PROTEIN; ESCRT III PROTEIN; ESCRT PROTEIN; F ACTIN; FILAMIN A; GAG PROTEIN; LIPOCORTIN 2; MATRIX PROTEIN; MESSENGER RNA; PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 80054813929     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.11.100     Document Type: Review
Times cited : (8)

References (150)
  • 1
    • 33845493481 scopus 로고    scopus 로고
    • Plasma membrane is the site of productive HIV-1 particle assembly
    • Jouvenet N, Neil SJ, Bess C, et al. Plasma membrane is the site of productive HIV-1 particle assembly. PLoS Biol. 4(12), e435 (2006
    • (2006) PLoS Biol. , vol.4 , Issue.12
    • Jouvenet, N.1    Neil, S.J.2    Bess, C.3
  • 2
    • 73149122533 scopus 로고    scopus 로고
    • Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles
    • Jouvenet N, Simon SM, Bieniasz PD. Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles. Proc. Natl Acad. Sci. USA 106(45), 19114-19119 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.45 , pp. 19114-19119
    • Jouvenet, N.1    Simon, S.M.2    Bieniasz, P.D.3
  • 3
    • 34447285254 scopus 로고    scopus 로고
    • Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane
    • DOI 10.1128/JVI.00308-07
    • Finzi A, Orthwein A, Mercier J, et al. Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane. J. Virol. 81(14), 7476-7490 (2007 (Pubitemid 47047835)
    • (2007) Journal of Virology , vol.81 , Issue.14 , pp. 7476-7490
    • Finzi, A.1    Orthwein, A.2    Mercier, J.3    Cohen, E.A.4
  • 6
    • 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. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316(5833), 1908-1912 (2007 (Pubitemid 47025792)
    • (2007) Science , vol.316 , Issue.5833 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 7
    • 34248229690 scopus 로고    scopus 로고
    • More than one door - Budding of enveloped viruses through cellular membranes
    • DOI 10.1016/j.febslet.2007.03.060, PII S0014579307003146, Membrane Trafficking
    • Welsch S, Muller, B, Krausslich HG. More than one door - budding of enveloped viruses through cellular membranes. FEBS Lett. 581(11), 2089-2097 (2007 (Pubitemid 46709908)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2089-2097
    • Welsch, S.1    Muller, B.2    Krausslich, H.-G.3
  • 8
    • 36248936657 scopus 로고    scopus 로고
    • Beyond Tsg101: The role of Alix in 'ESCRTing' HIV-1
    • DOI 10.1038/nrmicro1790, PII NRMICRO1790
    • Fujii K, Hurley JH, Freed EO. Beyond Tsg101: the role of Alix in ESCRTing HIV-1. Nat. Rev. Microbiol. 5(12), 912-916 (2007 (Pubitemid 350131179)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.12 , pp. 912-916
    • Fujii, K.1    Hurley, J.H.2    Freed, E.O.3
  • 9
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz PD. The cell biology of HIV-1 virion genesis. Cell Host Microbe 5(6), 550-558 (2009
    • (2009) Cell Host Microbe , vol.5 , Issue.6 , pp. 550-558
    • Bieniasz, P.D.1
  • 10
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor pr55(gag) virus-like particles from recombinant baculovirus-infected insect cells
    • DOI 10.1016/0092-8674(89)90873-8
    • Gheysen D, Jacobs E, de Foresta F, et al. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59(1), 103-112 (1989 (Pubitemid 19248562)
    • (1989) Cell , vol.59 , Issue.1 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 11
    • 79959211941 scopus 로고    scopus 로고
    • Host factors involved in retroviral budding and release
    • Martin-Serrano J, Neil SJ. Host factors involved in retroviral budding and release. Nat. Rev. Microbiol. 9(7), 519-531 (2011
    • (2011) Nat. Rev. Microbiol. , vol.9 , Issue.7 , pp. 519-531
    • Martin-Serrano, J.1    Neil, S.J.2
  • 13
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou W, Parent L, Wills J, et al. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68, 2556-2569 (1994
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.2    Wills, J.3
  • 16
    • 4143061388 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on Gag precursor-membrane interactions
    • DOI 10.1128/JVI.78.17.9560-9563.2004
    • Perez-Caballero D, Hatziioannou T, Martin-Serrano J, et al. Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions. J. Virol. 78(17), 9560-9563 (2004 (Pubitemid 39096563)
    • (2004) Journal of Virology , vol.78 , Issue.17 , pp. 9560-9563
    • Perez-Caballero, D.1    Hatziioannou, T.2    Martin-Serrano, J.3    Bieniasz, P.D.4
  • 17
    • 36349029236 scopus 로고    scopus 로고
    • Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells
    • DOI 10.1128/JVI.01280-07
    • Li H, Dou J, Ding L, et al. Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells. J. Virol. 81(23), 12899-12910 (2007 (Pubitemid 350156927)
    • (2007) Journal of Virology , vol.81 , Issue.23 , pp. 12899-12910
    • Li, H.1    Dou, J.2    Ding, L.3    Spearman, P.4
  • 19
    • 50049091709 scopus 로고    scopus 로고
    • Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting
    • Saad JS, Ablan SD, Ghanam RH, et al. Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting. J. Mol. Biol. 382(2), 434-447 (2008
    • (2008) J. Mol. Biol. , vol.382 , Issue.2 , pp. 434-447
    • Saad, J.S.1    Ablan, S.D.2    Ghanam, R.H.3
  • 22
    • 80051713783 scopus 로고    scopus 로고
    • The molecular architecture of HIV
    • Briggs JA, Krausslich HG. The molecular architecture of HIV. J. Mol. Biol. 410(4), 491-500 (2011
    • (2011) J. Mol. Biol. , vol.410 , Issue.4 , pp. 491-500
    • Briggs, J.A.1    Krausslich, H.G.2
  • 24
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • DOI 10.1038/sj.emboj.7601664, PII 7601664
    • Wright ER, Schooler JB, Ding HJ, et al. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 26(8), 2218-2226 (2007 (Pubitemid 46625799)
    • (2007) EMBO Journal , vol.26 , Issue.8 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6    Jensen, G.J.7
  • 25
    • 64849116750 scopus 로고    scopus 로고
    • HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate
    • Alfadhli A, Barklis RL, Barklis E. HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate. Virology 387(2), 466-472 (2009
    • (2009) Virology , vol.387 , Issue.2 , pp. 466-472
    • Alfadhli, A.1    Barklis, R.L.2    Barklis, E.3
  • 26
    • 80051766524 scopus 로고    scopus 로고
    • Structural determinants and mechanism of HIV-1 Genome Packaging
    • Lu K, Heng, X, Summers MF. Structural determinants and mechanism of HIV-1 Genome Packaging. J. Mol. Biol. 410(4), 609-633 (2011
    • (2011) J. Mol. Biol. , vol.410 , Issue.4 , pp. 609-633
    • Lu, K.1    Heng, X.2    Summers, M.F.3
  • 27
    • 78751670345 scopus 로고    scopus 로고
    • Properties and functions of the nucleocapsid protein in virus assembly
    • Muriaux, D, Darlix JL. Properties and functions of the nucleocapsid protein in virus assembly. RNA Biol. 7(6), 744-753 (2010
    • (2010) RNA Biol. , vol.7 , Issue.6 , pp. 744-753
    • Muriaux, D.1    Darlix, J.L.2
  • 28
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • Kutluay SB, Bieniasz PD. Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog. 6(11), e1001200 (2010
    • (2010) PLoS Pathog. , vol.6 , Issue.11
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 29
    • 79251517063 scopus 로고    scopus 로고
    • Cryo electron tomography of native HIV-1 budding sites
    • Carlson LA, de Marco A, Oberwinkler H, et al. Cryo electron tomography of native HIV-1 budding sites. PLoS Pathog. 6(11), e1001173 (2010
    • (2010) PLoS Pathog. , vol.6 , Issue.11
    • Carlson, L.A.1    De Marco, A.2    Oberwinkler, H.3
  • 30
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • DOI 10.1093/emboj/cdg143
    • Briggs JA, Wilk T, Welker R, et al. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 22(7), 1707-1715 (2003 (Pubitemid 36417418)
    • (2003) EMBO Journal , vol.22 , Issue.7 , pp. 1707-1715
    • Briggs, J.A.G.1    Wilk, T.2    Welker, R.3    Krausslich, H.-G.4    Fuller, S.D.5
  • 31
    • 34848866243 scopus 로고    scopus 로고
    • Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
    • DOI 10.1016/j.cell.2007.08.018, PII S0092867407010811
    • Ganser-Pornillos BK, Cheng A, Yeager M. Structure of full-length HIV-1 CA: a model for the mature capsid lattice. Cell 131(1), 70-79 (2007 (Pubitemid 47498532)
    • (2007) Cell , vol.131 , Issue.1 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 32
    • 79251521481 scopus 로고    scopus 로고
    • Structural analysis of HIV-1 maturation using cryo-electron tomography
    • de Marco A, Muller B, Glass B, et al. Structural analysis of HIV-1 maturation using cryo-electron tomography. PLoS Pathog. 6(11), e1001215 (2010
    • (2010) PLoS Pathog. , vol.6 , Issue.11
    • De Marco, A.1    Muller, B.2    Glass, B.3
  • 33
    • 0005241362 scopus 로고
    • Active human immunodeficiency virus protease is required for viral infectivity
    • Kohl NE, Emini EA, Schleif WA, et al. Active human immunodeficiency virus protease is required for viral infectivity. Proc. Natl Acad. Sci. USA 85(13), 4686-4690 (1988
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.13 , pp. 4686-4690
    • Kohl, N.E.1    Emini, E.A.2    Schleif, W.A.3
  • 35
    • 70350113492 scopus 로고    scopus 로고
    • HIV-1 Assembly at the plasma membrane: Gag trafficking and localization
    • Ono A. HIV-1 Assembly at the plasma membrane: Gag trafficking and localization. Future Virol. 4(3), 241-257 (2009
    • (2009) Future Virol. , vol.4 , Issue.3 , pp. 241-257
    • Ono, A.1
  • 36
    • 35148900054 scopus 로고    scopus 로고
    • Distinct intracellular trafficking of equine infectious anemia virus and human immunodeficiency virus type 1 gag during viral assembly and budding revealed by bimolecular fluorescence complementation assays
    • DOI 10.1128/JVI.00431-07
    • Jin J, Sturgeon T, Chen C, et al. Distinct intracellular trafficking of equine infectious anemia virus and human immunodeficiency virus type 1 Gag during viral assembly and budding revealed by bimolecular fluorescence complementation assays. J. Virol. 81 (20), 11226-11235 (2007 (Pubitemid 47536095)
    • (2007) Journal of Virology , vol.81 , Issue.20 , pp. 11226-11235
    • Jin, J.1    Sturgeon, T.2    Chen, C.3    Watkins, S.C.4    Weisz, O.A.5    Montelaro, R.C.6
  • 37
    • 68449098070 scopus 로고    scopus 로고
    • HIV-1 matrix dependent membrane targeting is regulated by Gag mRNA trafficking
    • Jin J, Sturgeon T, Weisz OA, et al. HIV-1 matrix dependent membrane targeting is regulated by Gag mRNA trafficking. PLoS ONE 4(8), e6551 (2009
    • (2009) PLoS ONE , vol.4 , Issue.8
    • Jin, J.1    Sturgeon, T.2    Weisz, O.A.3
  • 38
    • 38349130168 scopus 로고    scopus 로고
    • SOCS1 is an inducible host factor during HIV-1 infection and regulates the intracellular trafficking and stability of HIV-1 Gag
    • Ryo A, Tsurutani N, Ohba K, et al. SOCS1 is an inducible host factor during HIV-1 infection and regulates the intracellular trafficking and stability of HIV-1 Gag. Proc. Natl Acad. Sci. USA 105(1), 294-299 (2008
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.1 , pp. 294-299
    • Ryo, A.1    Tsurutani, N.2    Ohba, K.3
  • 39
    • 43049126181 scopus 로고    scopus 로고
    • GGA and Arf Proteins Modulate Retrovirus Assembly and Release
    • DOI 10.1016/j.molcel.2008.03.015, PII S1097276508002396
    • Joshi A, Garg H, Nagashima K, et al. GGA and Arf proteins modulate retrovirus assembly and release. Mol. Cell 30(2), 227-238 (2008 (Pubitemid 351626691)
    • (2008) Molecular Cell , vol.30 , Issue.2 , pp. 227-238
    • Joshi, A.1    Garg, H.2    Nagashima, K.3    Bonifacino, J.S.4    Freed, E.O.5
  • 40
    • 70449380150 scopus 로고    scopus 로고
    • Defects in cellular sorting and retroviral assembly induced by GGA overexpression
    • Joshi A, Nagashima, K, Freed EO. Defects in cellular sorting and retroviral assembly induced by GGA overexpression. BMC Cell Biol. 10, 72 (2009
    • (2009) BMC Cell Biol. , vol.10 , pp. 72
    • Joshi, A.1    Nagashima, K.2    Freed, E.O.3
  • 42
    • 27644598271 scopus 로고    scopus 로고
    • Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
    • DOI 10.1016/j.virol.2005.08.001, PII S0042682205004538
    • Batonick M, Favre M, Boge M, et al. Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2. Virology 342(2), 190-200 (2005 (Pubitemid 41566652)
    • (2005) Virology , vol.342 , Issue.2 , pp. 190-200
    • Batonick, M.1    Favre, M.2    Boge, M.3    Spearman, P.4    Honing, S.5    Thali, M.6
  • 44
    • 79959822636 scopus 로고    scopus 로고
    • Clathrin Facilitates the morphogenesis of retrovirus particles
    • Zhang F, Zang T, Wilson SJ, et al. Clathrin Facilitates the morphogenesis of retrovirus particles. PLoS Pathog. 7(6), e1002119 (2011
    • (2011) PLoS Pathog. , vol.7 , Issue.6
    • Zhang, F.1    Zang, T.2    Wilson, S.J.3
  • 45
    • 79952850908 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 and related primate lentiviruses engage clathrin through Gag-Pol or Gag
    • Popov S, Strack B, Sanchez-Merino V, et al. Human immunodeficiency virus type 1 and related primate lentiviruses engage clathrin through Gag-Pol or Gag. J. Virol. 85(8), 3792-3801 (2011
    • (2011) J. Virol. , vol.85 , Issue.8 , pp. 3792-3801
    • Popov, S.1    Strack, B.2    Sanchez-Merino, V.3
  • 46
    • 80051940629 scopus 로고    scopus 로고
    • Evidence of a role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) machinery in HIV-1 assembly and release
    • Joshi A, Garg H, Ablan SD, et al. Evidence of a role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) machinery in HIV-1 assembly and release. J. Biol. Chem. 286(34), 29861-29871 (2011)
    • (2011) J. Biol. Chem. , vol.286 , Issue.34 , pp. 29861-29871
    • Joshi, A.1    Garg, H.2    Ablan, S.D.3
  • 47
    • 79956098340 scopus 로고    scopus 로고
    • The cellular factors Vps18 and Mon2 are required for efficient production of infectious HIV-1 particles
    • Tomita Y, Noda T, Fujii K, et al. The cellular factors Vps18 and Mon2 are required for efficient production of infectious HIV-1 particles. J. Virol. 85(11), 5618-5627 (2011
    • (2011) J. Virol. , vol.85 , Issue.11 , pp. 5618-5627
    • Tomita, Y.1    Noda, T.2    Fujii, K.3
  • 48
    • 80051497830 scopus 로고    scopus 로고
    • Filamin a interacts with human immunodeficiency virus type 1 Gag and contributes to productive particle assembly
    • Cooper J, Liu L, Woodruff EA, et al. Filamin a interacts with human immunodeficiency virus type 1 Gag and contributes to productive particle assembly. J. Biol. Chem. 286(32), 28498-28510 (2011
    • (2011) J. Biol. Chem. , vol.286 , Issue.32 , pp. 28498-28510
    • Cooper, J.1    Liu, L.2    Woodruff, E.A.3
  • 49
    • 72249095705 scopus 로고    scopus 로고
    • Retroviral assembly and budding occur through an actin-driven mechanism
    • Gladnikoff M, Shimoni E, Gov NS, et al. Retroviral assembly and budding occur through an actin-driven mechanism. Biophys. J. 97(9), 2419-2428 (2009
    • (2009) Biophys. J. , vol.97 , Issue.9 , pp. 2419-2428
    • Gladnikoff, M.1    Shimoni, E.2    Gov, N.S.3
  • 50
    • 0036788110 scopus 로고    scopus 로고
    • Human Macrophages accumulate HIV-1 particles in MHC II compartments
    • Raposo GA, Moore M, Innes D, et al. Human Macrophages accumulate HIV-1 particles in MHC II compartments. Traffic 3(10), 718-729 (2002
    • (2002) Traffic , vol.3 , Issue.10 , pp. 718-729
    • Raposo, G.A.1    Moore, M.2    Innes, D.3
  • 51
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • DOI 10.1083/jcb.200304008
    • Pelchen-Matthews A, Kramer B, Marsh M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162(3), 443-455 (2003 (Pubitemid 36988553)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 52
    • 34547687819 scopus 로고    scopus 로고
    • HIV-1 Buds and Accumulates in "Nonacidic" Endosomes of Macrophages
    • DOI 10.1016/j.chom.2007.06.011, PII S193131280700159X
    • Jouve M, Sol-Foulon N, Watson S, et al. HIV-1 buds and accumulates in "nonacidic" endosomes of macrophages. Cell Host Microbe 2(2), 85-95 (2007 (Pubitemid 47209523)
    • (2007) Cell Host and Microbe , vol.2 , Issue.2 , pp. 85-95
    • Jouve, M.1    Sol-Foulon, N.2    Watson, S.3    Schwartz, O.4    Benaroch, P.5
  • 54
    • 33644768131 scopus 로고    scopus 로고
    • Annexin 2: A novel human immunodeficiency virus type 1 gag binding protein involved in replication in monocyte-derived macrophages
    • DOI 10.1128/JVI.80.6.2694-2704.2006
    • Ryzhova EV, Vos RM, Albright AV, et al. Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages. J. Virol. 80(6), 2694-2704 (2006 (Pubitemid 43346365)
    • (2006) Journal of Virology , vol.80 , Issue.6 , pp. 2694-2704
    • Ryzhova, E.V.1    Vos, R.M.2    Albright, A.V.3    Harrist, A.V.4    Harvey, T.5    Gonzalez-Scarano, F.6
  • 55
    • 63449114891 scopus 로고    scopus 로고
    • Anx2 interacts with HIV-1 Gag at phosphatidylinositol(4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells
    • Harrist AV, Ryzhova EV, Harvey T, et al. Anx2 interacts with HIV-1 Gag at phosphatidylinositol(4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells. PLoS ONE 4(3), e5020 (2009
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Harrist, A.V.1    Ryzhova, E.V.2    Harvey, T.3
  • 56
    • 34047225272 scopus 로고    scopus 로고
    • HIV-1 buds predominantly at the plasma membrane of primary human macrophages
    • Welsch S, Keppler OT, Habermann A, et al. HIV-1 buds predominantly at the plasma membrane of primary human macrophages. PLoS Pathog. 3(3), e36 (2007
    • (2007) PLoS Pathog. , vol.3 , Issue.3
    • Welsch, S.1    Keppler, O.T.2    Habermann, A.3
  • 57
    • 34247529467 scopus 로고    scopus 로고
    • In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53
    • DOI 10.1083/jcb.200609050
    • Deneka M, Pelchen-Matthews A, Byland R, et al. In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53. J. Cell Biol. 177(2), 329-341 (2007 (Pubitemid 46658643)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 329-341
    • Deneka, M.1    Pelchen-Matthews, A.2    Byland, R.3    Ruiz-Mateos, E.4    Marsh, M.5
  • 58
    • 70349686333 scopus 로고    scopus 로고
    • Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages
    • Bennett AE, Narayan K, Shi D, et al. Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages. PLoS Pathog. 5(9), e1000591 (2009
    • (2009) PLoS Pathog. , vol.5 , Issue.9
    • Bennett, A.E.1    Narayan, K.2    Shi, D.3
  • 59
    • 79960428430 scopus 로고    scopus 로고
    • Architecture and regulation of the HIV-1 assembly and holding compartment in macrophages
    • Welsch S, Groot F, Krausslich H-G, et al. Architecture and regulation of the HIV-1 assembly and holding compartment in macrophages. J. Virol. 85(15), 7922-7927 (2011
    • (2011) J. Virol. , vol.85 , Issue.15 , pp. 7922-7927
    • Welsch, S.1    Groot, F.2    Krausslich, H.-G.3
  • 61
    • 0028971135 scopus 로고
    • P6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M, Orenstein J, Martin M, et al. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69, 6810-6818 (1995
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.2    Martin, M.3
  • 62
    • 0029092338 scopus 로고
    • Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Parent L, Bennett R, Craven R, et al. Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J. Virol. 69, 5455-5460 (1995
    • (1995) J. Virol. , vol.69 , pp. 5455-5460
    • Parent, L.1    Bennett, R.2    Craven, R.3
  • 63
    • 0036094492 scopus 로고    scopus 로고
    • Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis
    • DOI 10.1128/JVI.76.11.5472-5479.2002
    • Strack B, Calistri, A, Gottlinger HG. Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis. J. Virol. 76(11), 5472-5479 (2002 (Pubitemid 34517897)
    • (2002) Journal of Virology , vol.76 , Issue.11 , pp. 5472-5479
    • Strack, B.1    Calistri, A.2    Gottlinger, H.G.3
  • 64
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • DOI 10.1128/JVI.78.11.5554-5563.2004
    • Martin-Serrano J, Perez-Caballero D, Bieniasz PD. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78(11), 5554-5563 (2004 (Pubitemid 38661642)
    • (2004) Journal of Virology , vol.78 , Issue.11 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 65
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • DOI 10.1016/j.virusres.2004.08.007, PII S0168170204003181
    • Demirov DG, Freed EO. Retrovirus budding. Virus Res. 106(2), 87-102 (2004 (Pubitemid 39582739)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC. ISS. , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 66
    • 59749099366 scopus 로고    scopus 로고
    • The ESCRT pathway and HIV-1 budding
    • Usami Y, Popov S, Popova E, et al. The ESCRT pathway and HIV-1 budding. Biochem. Soc. Trans. 37(Pt 1), 181-184 (2009
    • (2009) Biochem. Soc. Trans. , vol.37 , Issue.PART 1 , pp. 181-184
    • Usami, Y.1    Popov, S.2    Popova, E.3
  • 67
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • DOI 10.1016/j.virol.2005.09.044, PII S0042682205005994
    • Bieniasz PD. Late budding domains and host proteins in enveloped virus release. Virology 344(1), 55-63 (2006 (Pubitemid 41814450)
    • (2006) Virology , vol.344 , Issue.1 , pp. 55-63
    • Bieniasz, P.D.1
  • 68
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • DOI 10.1016/j.virol.2005.09.018, PII S0042682205005878
    • Hartlieb B, Weissenhorn W. Filovirus assembly and budding. Virology 344(1), 64-70 (2006 (Pubitemid 41814451)
    • (2006) Virology , vol.344 , Issue.1 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 69
    • 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, et al. ESCRTing proteins in the endocytic pathway. Trends Biochem. Sci. 32(12), 561-573 (2007 (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
  • 70
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery: Its all in the neck
    • Hurley JH, Hanson PI. Membrane budding and scission by the ESCRT machinery: its all in the neck. Nat. Rev. Mol. Cell. Biol. 11(8), 556-566 (2010
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , Issue.8 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 71
    • 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. Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 26(19), 4215-4227 (2007 (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
  • 72
    • 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. Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. Proc. Natl Acad. Sci. USA 107, 12889-12894 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 12889-12894
    • Morita, E.1    Colf, L.A.2    Karren, M.A.3
  • 73
    • 79953161074 scopus 로고    scopus 로고
    • Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments
    • Guizetti J, Schermelleh L, Mantler J, et al. Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments. Science 331(6024), 1616-1620 (2011
    • (2011) Science , vol.331 , Issue.6024 , pp. 1616-1620
    • Guizetti, J.1    Schermelleh, L.2    Mantler, J.3
  • 74
    • 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. Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission. Proc. Natl Acad. Sci. USA 108(12), 4846- 4851 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , Issue.12 , pp. 4846-4851
    • Elia, N.1    Sougrat, R.2    Spurlin, T.A.3
  • 76
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • DOI 10.1038/nm1201-1313
    • Martin-Serrano J, Zang T, Bieniasz P. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7, 1313-1319 (2001 (Pubitemid 34007935)
    • (2001) Nature Medicine , vol.7 , Issue.12 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 78
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • DOI 10.1016/S0092-8674(03)00653-6
    • Strack B, Calistri A, Popova E, et al. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114, 689-699 (2003 (Pubitemid 37186765)
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 81
    • 0037370013 scopus 로고    scopus 로고
    • YPXL/I is a protein interaction motif recognized by Aspergillus PalA and its human homologue, AIP1/Alix
    • DOI 10.1128/MCB.23.5.1647-1655.2003
    • Vincent O, Rainbow L, Tilburn J, et al. YPXL/I is a protein interaction motif recognized by aspergillus PalA and its human homologue, AIP1/Alix. Mol. Cell Biol. 23(5), 1647-1655 (2003 (Pubitemid 36246046)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.5 , pp. 1647-1655
    • Vincent, O.1    Rainbow, L.2    Tilburn, J.3    Arst Jr., H.N.4    Penalva, M.A.5
  • 82
    • 0034700097 scopus 로고    scopus 로고
    • A role for ubiquitin ligase recruitment in retrovirus release
    • Strack B, Calistri A, Accola M, et al. A role for ubiquitin ligase recruitment in retrovirus release. Proc. Natl Acad. Sci. USA 97, 13063-13068 (2000
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13063-13068
    • Strack, B.1    Calistri, A.2    Accola, M.3
  • 83
    • 0036023945 scopus 로고    scopus 로고
    • Functional involvement of a novel Nedd4-like ubiquitin ligase on retrovirus budding
    • Yasuda J, Hunter E, Nakao M, et al. Functional involvement of a novel Nedd4-like ubiquitin ligase on retrovirus budding. EMBO Rep. 3(7), 636-640 (2002
    • (2002) EMBO Rep. , vol.3 , Issue.7 , pp. 636-640
    • Yasuda, J.1    Hunter, E.2    Nakao, M.3
  • 84
    • 0242331750 scopus 로고    scopus 로고
    • PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101
    • DOI 10.1128/JVI.77.22.11882-11895.2003
    • Bouamr F, Melillo JA, Wang MQ, et al. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]. J. Virol. 77(22), 11882-11895 (2003 (Pubitemid 37339842)
    • (2003) Journal of Virology , vol.77 , Issue.22 , pp. 11882-11895
    • Bouamr, F.1    Melillo, J.A.2    Wang, M.Q.3    Nagashima, K.4    De Los Santos, M.5    Rein, A.6    Goff, S.P.7
  • 85
    • 33847355934 scopus 로고    scopus 로고
    • Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding
    • DOI 10.1016/j.cell.2007.01.035, PII S0092867407001808
    • Fisher RD, Chung HY, Zhai Q, et al. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128(5), 841-852 (2007 (Pubitemid 46341413)
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.-Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 86
    • 68549139876 scopus 로고    scopus 로고
    • Functional role of Alix in HIV-1 replication
    • Fujii K, Munshi UM, Ablan SD, et al. Functional role of Alix in HIV-1 replication. Virology 391(2), 284-292 (2009
    • (2009) Virology , vol.391 , Issue.2 , pp. 284-292
    • Fujii, K.1    Munshi, U.M.2    Ablan, S.D.3
  • 89
    • 37849024338 scopus 로고    scopus 로고
    • Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV
    • Zhai Q, Fisher RD, Chung HY, et al. Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV. Nat. Struct. Mol. Biol. 15(1), 43-49 (2008
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.1 , pp. 43-49
    • Zhai, Q.1    Fisher, R.D.2    Chung, H.Y.3
  • 90
    • 33748302008 scopus 로고    scopus 로고
    • The multiple personalities of Alix
    • DOI 10.1242/jcs.03072
    • Odorizzi G. The multiple personalities of Alix. J. Cell Sci. 119(15), 3025-3032 (2006 (Pubitemid 44322116)
    • (2006) Journal of Cell Science , vol.119 , Issue.15 , pp. 3025-3032
    • Odorizzi, G.1
  • 91
    • 61449173915 scopus 로고    scopus 로고
    • The CHMP4b-and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix
    • Zhou X, Pan S, Sun L, et al. The CHMP4b-and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix. Biochem. J. 418(2), 277-284 (2009
    • (2009) Biochem. J. , vol.418 , Issue.2 , pp. 277-284
    • Zhou, X.1    Pan, S.2    Sun, L.3
  • 92
    • 80052293740 scopus 로고    scopus 로고
    • Activation of the retroviral budding factor ALIX
    • Zhai Q, Landesman MB, Chung HY, et al. activation of the retroviral budding factor ALIX. J. Virol. 85(17), 9222-9226 (2011
    • (2011) J. Virol. , vol.85 , Issue.17 , pp. 9222-9226
    • Zhai, Q.1    Landesman, M.B.2    Chung, H.Y.3
  • 93
    • 66749147856 scopus 로고    scopus 로고
    • A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments
    • Pires R, Hartlieb B, Signor L, et al. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure 17(6), 843-856 (2009
    • (2009) Structure , vol.17 , Issue.6 , pp. 843-856
    • Pires, R.1    Hartlieb, B.2    Signor, L.3
  • 94
    • 33947544434 scopus 로고    scopus 로고
    • An Alix fragment potently inhibits HIV-1 budding: Characterization of binding to retroviral YPXL late domains
    • DOI 10.1074/jbc.M607489200
    • Munshi UM, Kim J, Nagashima K, et al. An Alix fragment potently inhibits HIV-1 budding: characterization of binding to retroviral YPXL late domains. J. Biol. Chem. 282(6), 3847-3855 (2007 (Pubitemid 47084496)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3847-3855
    • Munshi, U.M.1    Kim, J.2    Nagashima, K.3    Hurley, J.H.4    Freed, E.O.5
  • 95
    • 34249943479 scopus 로고    scopus 로고
    • Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site
    • DOI 10.1128/JVI.00314-07
    • Usami Y, Popov S, Gottlinger HG. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J. Virol. 81(12), 6614-6622 (2007 (Pubitemid 46878065)
    • (2007) Journal of Virology , vol.81 , Issue.12 , pp. 6614-6622
    • Usami, Y.1    Popov, S.2    Gottlinger, H.G.3
  • 96
    • 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. Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release. Proc. Natl Acad. Sci. USA 105(30), 10541-10546 (2008
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.30 , pp. 10541-10546
    • Carlton, J.G.1    Agromayor, M.2    Martin-Serrano, J.3
  • 97
    • 38349174466 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP 1 through the nucleocapsid
    • Popov S, Popova E, Inoue M, et al. Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid. J. Virol. 82(3), 1389-1398 (2008
    • (2008) J. Virol. , vol.82 , Issue.3 , pp. 1389-1398
    • Popov, S.1    Popova, E.2    Inoue, M.3
  • 98
    • 63449121941 scopus 로고    scopus 로고
    • The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding
    • Dussupt V, Javid MP, Abou-Jaoude G, et al. The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding. PLoS Pathog. 5(3), e1000339 (2009
    • (2009) PLoS Pathog. , vol.5 , Issue.3
    • Dussupt, V.1    Javid, M.P.2    Abou-Jaoude, G.3
  • 99
    • 79551702980 scopus 로고    scopus 로고
    • Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding
    • Dussupt V, Sette P, Bello NF, et al. Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding. J. Virol. 85(5), 2304-2315 (2011
    • (2011) J. Virol. , vol.85 , Issue.5 , pp. 2304-2315
    • Dussupt, V.1    Sette, P.2    Bello, N.F.3
  • 100
    • 77953319640 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid p1 confers ESCRT pathway dependence
    • Popova E, Popov, S, Gottlinger HG. Human immunodeficiency virus type 1 nucleocapsid p1 confers ESCRT pathway dependence. J. Virol. 84(13), 6590-6597 (2010
    • (2010) J. Virol. , vol.84 , Issue.13 , pp. 6590-6597
    • Popova, E.1    Popov, S.2    Gottlinger, H.G.3
  • 101
    • 67650451138 scopus 로고    scopus 로고
    • Divergent Bro1 domains share the capacity to bind human immunodeficiency virus type 1 nucleocapsid and to enhance virus-like particle production
    • Popov S, Popova E, Inoue M, et al. Divergent Bro1 domains share the capacity to bind human immunodeficiency virus type 1 nucleocapsid and to enhance virus-like particle production. J. Virol. 83(14), 7185-7193 (2009
    • (2009) J. Virol. , vol.83 , Issue.14 , pp. 7185-7193
    • Popov, S.1    Popova, E.2    Inoue, M.3
  • 102
    • 34548580258 scopus 로고    scopus 로고
    • The role of ubiquitin in retroviral egress
    • DOI 10.1111/j.1600-0854.2007.00609.x
    • Martin-Serrano J. The role of ubiquitin in retroviral egress. Traffic 8(10), 1297-1303 (2007 (Pubitemid 47394235)
    • (2007) Traffic , vol.8 , Issue.10 , pp. 1297-1303
    • Martin-Serrano, J.1
  • 103
    • 34548155408 scopus 로고    scopus 로고
    • Ubiquitination of human immunodeficiency virus type 1 gag is highly dependent on gag membrane association
    • DOI 10.1128/JVI.00044-07
    • Jager S, Gottwein, E, Krausslich HG. Ubiquitination of human immunodeficiency virus type 1 Gag is highly dependent on Gag membrane association. J. Virol. 81(17), 9193-9201 (2007 (Pubitemid 47311462)
    • (2007) Journal of Virology , vol.81 , Issue.17 , pp. 9193-9201
    • Jager, S.1    Gottwein, E.2    Krausslich, H.-G.3
  • 104
    • 43249121457 scopus 로고    scopus 로고
    • NEDD4L overexpression rescues the release and infectivity of human immunodeficiency virus type 1 constructs lacking PTAP and YPXL late domains
    • DOI 10.1128/JVI.02667-07
    • Chung HY, Morita E, von Schwedler U, et al. NEDD4L overexpression rescues the release and infectivity of human immunodeficiency virus type 1 constructs lacking PTAP and YPXL late domains. J. Virol. 82(10), 4884-4897 (2008 (Pubitemid 351657050)
    • (2008) Journal of Virology , vol.82 , Issue.10 , pp. 4884-4897
    • Chung, H.-Y.1    Morita, E.2    Von Schwedler, U.3    Muller, B.4    Krausslich, H.-G.5    Sundquist, W.I.6
  • 105
    • 43249110449 scopus 로고    scopus 로고
    • Efficient and specific rescue of human immunodeficiency virus type 1 budding defects by a Nedd4-like ubiquitin ligase
    • DOI 10.1128/JVI.02675-07
    • Usami Y, Popov S, Popova E, et al. Efficient and specific rescue of human immunodeficiency virus type 1 budding defects by a Nedd4-like ubiquitin ligase. J. Virol. 82, 4898-4907 (2008 (Pubitemid 351657051)
    • (2008) Journal of Virology , vol.82 , Issue.10 , pp. 4898-4907
    • Usami, Y.1    Popov, S.2    Popova, E.3    Gottlinger, H.G.4
  • 106
    • 78449244125 scopus 로고    scopus 로고
    • Functional interchangeability of late domains, late domain cofactors and ubiquitin in viral budding
    • Zhadina M, Bieniasz PD. Functional interchangeability of late domains, late domain cofactors and ubiquitin in viral budding. PLoS Pathog. 6(10), e1001153 (2010
    • (2010) PLoS Pathog. , vol.6 , Issue.10
    • Zhadina, M.1    Bieniasz, P.D.2
  • 107
    • 78149301835 scopus 로고    scopus 로고
    • Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag
    • Weiss ER, Popova E, Yamanaka H, et al. Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag. PLoS Pathog. 6(9) e1001107 (2010
    • (2010) PLoS Pathog. , vol.6 , Issue.9
    • Weiss, E.R.1    Popova, E.2    Yamanaka, H.3
  • 108
    • 12144258074 scopus 로고    scopus 로고
    • HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway
    • DOI 10.1083/jcb.200408155
    • Martin-Serrano J, Eastman SW, Chung W, et al. HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway. J. Cell Biol. 168(1), 89-101 (2005 (Pubitemid 40111060)
    • (2005) Journal of Cell Biology , vol.168 , Issue.1 , pp. 89-101
    • Martin-Serrano, J.1    Eastman, S.W.2    Chung, W.3    Bieniasz, P.D.4
  • 109
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell. Biol. 10(8), 550-563 (2009
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , Issue.8 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 110
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo
    • Agromayor M, Martin-Serrano J. Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. J. Biol. Chem. 281(32), 23083-23091 (2006
    • (2006) J. Biol. Chem. , vol.281 , Issue.32 , pp. 23083-23091
    • Agromayor, M.1    Martin-Serrano, J.2
  • 112
    • 80051495469 scopus 로고    scopus 로고
    • Structural basis for ESCRT-III CHMP3 recruitment of AMSH
    • Solomons J, Sabin C, Poudevigne E, et al. Structural basis for ESCRT-III CHMP3 recruitment of AMSH. Structure 19(18), 1149-1159 (2011
    • (2011) Structure , vol.19 , Issue.18 , pp. 1149-1159
    • Solomons, J.1    Sabin, C.2    Poudevigne, E.3
  • 113
    • 53849141487 scopus 로고    scopus 로고
    • Functional replacement of a retroviral late domain by ubiquitin fusion
    • Joshi A, Munshi U, Ablan SD, et al. Functional replacement of a retroviral late domain by ubiquitin fusion. Traffic 9(11), 1972-1983 (2008
    • (2008) Traffic , vol.9 , Issue.11 , pp. 1972-1983
    • Joshi, A.1    Munshi, U.2    Ablan, S.D.3
  • 114
    • 79952850905 scopus 로고    scopus 로고
    • Identification of an inhibitory budding signal that blocks the release of HIV particles and exosome/microvesicle proteins
    • Gan X, Gould SJ. Identification of an inhibitory budding signal that blocks the release of HIV particles and exosome/microvesicle proteins. Mol. Biol. Cell 22(6), 817-830 (2011
    • (2011) Mol. Biol. Cell , vol.22 , Issue.6 , pp. 817-830
    • Gan, X.1    Gould, S.J.2
  • 115
    • 79952753922 scopus 로고    scopus 로고
    • TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding through targeting endosomal sorting complex required for transport-I
    • Da Q, Yang X, Xu Y, et al. TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding through targeting endosomal sorting complex required for transport-I. J. Immunol. 186(5), 3023-3030 (2011
    • (2011) J. Immunol. , vol.186 , Issue.5 , pp. 3023-3030
    • Da Yang Q, X.1    Xu, Y.2
  • 117
    • 68449095867 scopus 로고    scopus 로고
    • Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis
    • Im YJ, Wollert T, Boura E, et al. Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev. Cell 17(2), 234-243 (2009
    • (2009) Dev. Cell , vol.17 , Issue.2 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3
  • 118
  • 119
    • 33745761343 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment
    • Pineda-Molina E, Belrhali H, Piefer AJ, et al. The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Traffic 7(8), 1007-1016 (2006
    • (2006) Traffic , vol.7 , Issue.8 , pp. 1007-1016
    • Pineda-Molina, E.1    Belrhali, H.2    Piefer, A.J.3
  • 120
    • 79960391953 scopus 로고    scopus 로고
    • Sprouty 2 binds ESCRT-II factor Eap20 and facilitates HIV-1 Gag release
    • Medina GN, Ehrlich LS, Chen MH, et al. Sprouty 2 binds ESCRT-II factor Eap20 and facilitates HIV-1 Gag release. J. Virol. 85(14), 7353-7362 (2011
    • (2011) J. Virol. , vol.85 , Issue.14 , pp. 7353-7362
    • Medina, G.N.1    Ehrlich, L.S.2    Chen, M.H.3
  • 121
    • 80052646441 scopus 로고    scopus 로고
    • Regulation of Vps4 during MVB sorting and cytokinesis
    • Davies BA, Babst M, Katzmann DJ. Regulation of Vps4 during MVB sorting and cytokinesis. Traffic 12(10), 1298-1305 (2011
    • (2011) Traffic , vol.12 , Issue.10 , pp. 1298-1305
    • Davies, B.A.1    Babst, M.2    Katzmann, D.J.3
  • 122
    • 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, et al. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17(11), 2982-2993 (1998 (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
  • 123
    • 16844375707 scopus 로고    scopus 로고
    • Interaction of the mammalian endosomal sorting complex required for transport(ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1
    • Lin Y, Kimpler LA, Naismith TV, et al. Interaction of the mammalian endosomal sorting complex required for transport(ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1. J. Biol. Chem. 280(13), 12799-12809 (2005
    • (2005) J. Biol. Chem. , vol.280 , Issue.13 , pp. 12799-12809
    • Lin, Y.1    Kimpler, L.A.2    Naismith, T.V.3
  • 124
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • Saksena S, Wahlman J, Teis D, et al. Functional reconstitution of ESCRT-III assembly and disassembly. Cell 136(1), 97-109 (2009
    • (2009) Cell , vol.136 , Issue.1 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3
  • 125
    • 79954417888 scopus 로고    scopus 로고
    • Divergent pathways lead to ESCRT-III catalyzed membrane fission
    • Peel S, Macheboeuf P, Martinelli N, et al. Divergent pathways lead to ESCRT-III catalyzed membrane fission. Trends Biochem. Sci. 36((4)), 199-210 (2011
    • (2011) Trends Biochem. Sci. , vol.36 , Issue.4 , pp. 199-210
    • Peel, S.1    MacHeboeuf, P.2    Martinelli, N.3
  • 127
    • 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. Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 8(8), 1068-1079 (2007 (Pubitemid 47074039)
    • (2007) Traffic , vol.8 , Issue.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 128
    • 41949105167 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of ESCRT-III CHMP3
    • Lata S, Roessle M, Solomons J, et al. Structural basis for autoinhibition of ESCRT-III CHMP3. J. Mol. Biol. 378(4), 818-827 (2008
    • (2008) J. Mol. Biol. , vol.378 , Issue.4 , pp. 818-827
    • Lata, S.1    Roessle, M.2    Solomons, J.3
  • 129
    • 67650312119 scopus 로고    scopus 로고
    • Structural basis for ESCRT-III protein autoinhibition
    • Bajorek M, Schubert HL, McCullough J, et al. Structural basis for ESCRT-III protein autoinhibition. Nat. Struct. Mol. Biol. 16(7), 754-762 (2009
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , Issue.7 , pp. 754-762
    • Bajorek, M.1    Schubert, H.L.2    McCullough, J.3
  • 130
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • Rozycki B, Kim YC, Hummer G. SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions. Structure 19(1), 109-116 (2011
    • (2011) Structure , vol.19 , Issue.1 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 132
    • 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. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449(7163), 735-739 (2007 (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
  • 133
    • 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. Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev. Cell 15(1), 62-73 (2008 (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
  • 134
    • 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, et al. Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J. Cell Biol. 180(2), 389-402 (2008 (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
  • 135
    • 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. Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24. Structure 16(9), 1345-1356 (2008
    • (2008) Structure , vol.16 , Issue.9 , pp. 1345-1356
    • Ghazi-Tabatabai, S.1    Saksena, S.2    Short, J.M.3
  • 136
    • 51149106799 scopus 로고    scopus 로고
    • Helical structures of ESCRT-III are disassembled by VPS4
    • Lata S, Schoehn G, Jain A, et al. Helical structures of ESCRT-III are disassembled by VPS4. Science 321(5894), 1354-1357 (2008
    • (2008) Science , vol.321 , Issue.5894 , pp. 1354-1357
    • Lata, S.1    Schoehn, G.2    Jain, A.3
  • 137
    • 73449092185 scopus 로고    scopus 로고
    • Computational model of membrane fission catalyzed by ESCRT-III
    • Fabrikant G, Lata S, Riches JD, et al. Computational model of membrane fission catalyzed by ESCRT-III. PLoS Comput. Biol. 5(11), e1000575 (2009
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.11
    • Fabrikant, G.1    Lata, S.2    Riches, J.D.3
  • 139
    • 62249210955 scopus 로고    scopus 로고
    • Membrane scission by the ESCRT-III complex
    • Wollert T, Wunder C, Lippincott-Schwartz J, et al. Membrane scission by the ESCRT-III complex. Nature 458(7235), 172-177 (2009
    • (2009) Nature , vol.458 , Issue.7235 , pp. 172-177
    • Wollert, T.1    Wunder, C.2    Lippincott-Schwartz, J.3
  • 140
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert T, Hurley JH. Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464(7290), 864-869. (2010
    • (2010) Nature , vol.464 , Issue.7290 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 141
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • DOI 10.1038/nature06998, PII NATURE06998
    • Jouvenet N, Bieniasz PD, Simon SM. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 454(7201), 236-240 (2008 (Pubitemid 351969887)
    • (2008) Nature , vol.454 , Issue.7201 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 142
    • 79953296191 scopus 로고    scopus 로고
    • Dynamics of ESCRT protein recruitment during retroviral assembly
    • Jouvenet N, Zhadina M, Bieniasz PD, et al. Dynamics of ESCRT protein recruitment during retroviral assembly. Nat. Cell Biol. 13(4), 394-401 (2011
    • (2011) Nat. Cell Biol. , vol.13 , Issue.4 , pp. 394-401
    • Jouvenet, N.1    Zhadina, M.2    Bieniasz, P.D.3
  • 143
    • 79953323443 scopus 로고    scopus 로고
    • Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component
    • Baumgartel V, Ivanchenko S, Dupont A, et al. Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component. Nat. Cell Biol. 13(4), 469-474 (2011
    • (2011) Nat. Cell Biol. , vol.13 , Issue.4 , pp. 469-474
    • Baumgartel, V.1    Ivanchenko, S.2    Dupont, A.3
  • 144
    • 79952640255 scopus 로고    scopus 로고
    • ESCRT-III protein requirements for HIV-1 budding
    • Morita E, Sandrin V, McCullough J, et al. ESCRT-III protein requirements for HIV-1 budding. Cell Host Microbe 9(3), 235-242 (2011
    • (2011) Cell Host Microbe , vol.9 , Issue.3 , pp. 235-242
    • Morita, E.1    Sandrin, V.2    McCullough, J.3
  • 146
    • 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, et al. ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation. EMBO J. 29(5), 871-883 (2010
    • (2010) EMBO J. , vol.29 , Issue.5 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3
  • 147
    • 78650636013 scopus 로고    scopus 로고
    • Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure
    • Ghanam RH, Fernandez TF, Fledderman EL, et al. Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure. J. Biol. Chem. 285(53), 41911-41920 (2011
    • (2011) J. Biol. Chem. , vol.285 , Issue.53 , pp. 41911-41920
    • Ghanam, R.H.1    Fernandez, T.F.2    Fledderman, E.L.3
  • 149
    • 33645231680 scopus 로고    scopus 로고
    • Basic residues in the nucleocapsid domain of Gag are required for interaction of HIV-1 Gag with ABCE1 (HP68), a cellular protein important for HIV-1 capsid assembly
    • DOI 10.1074/jbc.M507255200
    • Lingappa JR, Dooher JE, Newman MA, et al. Basic residues in the nucleocapsid domain of Gag are required for interaction of HIV-1 gag with ABCE1(HP68), a cellular protein important for HIV-1 capsid assembly. J. Biol. Chem. 281(7), 3773-3784 (2006 (Pubitemid 43847801)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 3773-3784
    • Lingappa, J.R.1    Dooher, J.E.2    Newman, M.A.3    Kiser, P.K.4    Klein, K.C.5
  • 150
    • 63049134547 scopus 로고    scopus 로고
    • Human discs large is a new negative regulator of human immunodeficiency virus-1 infectivity
    • Perugi F, Muriaux D, Ramirez BC, et al. Human discs large is a new negative regulator of human immunodeficiency virus-1 infectivity. Mol. Biol. Cell 20(1), 498-508 (2009
    • (2009) Mol. Biol. Cell , vol.20 , Issue.1 , pp. 498-508
    • Perugi, F.1    Muriaux, D.2    Ramirez, B.C.3


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