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Volumn 20, Issue 5, 2012, Pages 874-886

Solution structure of the ESCRT-I and -II supercomplex: Implications for membrane budding and scission

Author keywords

[No Author keywords available]

Indexed keywords

ESCRT PROTEIN;

EID: 84861083754     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.03.008     Document Type: Article
Times cited : (78)

References (56)
  • 2
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • M. Babst, D.J. Katzmann, E.J. Estepa-Sabal, T. Meerloo, and S.D. Emr Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting Dev. Cell 3 2002 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
  • 3
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • M. Babst, D.J. Katzmann, W.B. Snyder, B. Wendland, and S.D. Emr Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body Dev. Cell 3 2002 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
  • 4
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • DOI 10.1083/jcb.200302131
    • K.G. Bache, A. Brech, A. Mehlum, and H. Stenmark Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes J. Cell Biol. 162 2003 435 442 (Pubitemid 36988552)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 6
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • DOI 10.1083/jcb.200305007
    • P.S. Bilodeau, S.C. Winistorfer, W.R. Kearney, A.D. Robertson, and R.C. Piper Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome J. Cell Biol. 163 2003 237 243 (Pubitemid 37363125)
    • (2003) Journal of Cell Biology , vol.163 , Issue.2 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 8
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • DOI 10.1126/science.1143422
    • J.G. Carlton, and J. Martin-Serrano Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery Science 316 2007 1908 1912 (Pubitemid 47025792)
    • (2007) Science , vol.316 , Issue.5833 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 9
    • 67749147584 scopus 로고    scopus 로고
    • Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories
    • H.S. Chung, J.M. Louis, and W.A. Eaton Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories Proc. Natl. Acad. Sci. USA 106 2009 11837 11844
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11837-11844
    • Chung, H.S.1    Louis, J.M.2    Eaton, W.A.3
  • 10
    • 79953225554 scopus 로고    scopus 로고
    • Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission
    • N. Elia, R. Sougrat, T. Spurlin, J.H. Hurley, and J. Lippincott-Schwartz Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission Proc. Natl. Acad. Sci. USA 108 2011 4846 4851
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4846-4851
    • Elia, N.1    Sougrat, R.2    Spurlin, T.3    Hurley, J.H.4    Lippincott-Schwartz, J.5
  • 12
    • 33846517041 scopus 로고    scopus 로고
    • Structural insight into the ESCRT-I/-II link and its role in MVB trafficking
    • DOI 10.1038/sj.emboj.7601501, PII 7601501
    • D.J. Gill, H. Teo, J. Sun, O. Perisic, D.B. Veprintsev, S.D. Emr, and R.L. Williams Structural insight into the ESCRT-I/-II link and its role in MVB trafficking EMBO J. 26 2007 600 612 (Pubitemid 46160959)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 600-612
    • Gill, D.J.1    Teo, H.2    Sun, J.3    Perisic, O.4    Veprintsev, D.B.5    Emr, S.D.6    Williams, R.L.7
  • 13
    • 36249028655 scopus 로고    scopus 로고
    • Single-molecule FRET with diffusion and conformational dynamics
    • DOI 10.1021/jp075255e
    • I.V. Gopich, and A. Szabo Single-molecule FRET with diffusion and conformational dynamics J. Phys. Chem. B 111 2007 12925 12932 (Pubitemid 350136484)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.44 , pp. 12925-12932
    • Gopich, I.V.1    Szabo, A.2
  • 14
    • 44949226031 scopus 로고    scopus 로고
    • Concentration effects in "single-molecule" spectroscopy
    • I.V. Gopich Concentration effects in "single-molecule" spectroscopy J. Phys. Chem. B 112 2008 6214 6220
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6214-6220
    • Gopich, I.V.1
  • 15
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • DOI 10.1083/jcb.200707031
    • P.I. Hanson, R. Roth, Y. Lin, and J.E. Heuser Plasma membrane deformation by circular arrays of ESCRT-III protein filaments J. Cell Biol. 180 2008 389 402 (Pubitemid 351185923)
    • (2008) Journal of Cell Biology , vol.180 , Issue.2 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 16
    • 4544255838 scopus 로고    scopus 로고
    • Structure of the ESCRT-II endosomal trafficking complex
    • DOI 10.1038/nature02914
    • A. Hierro, J. Sun, A.S. Rusnak, J. Kim, G. Prag, S.D. Emr, and J.H. Hurley Structure of the ESCRT-II endosomal trafficking complex Nature 431 2004 221 225 (Pubitemid 39243478)
    • (2004) Nature , vol.431 , Issue.7005 , pp. 221-225
    • Hierro, A.1    Sun, J.I.2    Rusnak, A.S.3    Kim, J.4    Prag, G.5    Emr, S.O.6    Hurley, J.H.7
  • 17
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery: It's all in the neck
    • J.H. Hurley, and P.I. Hanson Membrane budding and scission by the ESCRT machinery: it's all in the neck Nat. Rev. Mol. Cell Biol. 11 2010 556 566
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 18
    • 44449097226 scopus 로고    scopus 로고
    • Integrated Structural Model and Membrane Targeting Mechanism of the Human ESCRT-II Complex
    • DOI 10.1016/j.devcel.2008.04.004, PII S1534580708001676
    • Y.J. Im, and J.H. Hurley Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex Dev. Cell 14 2008 902 913 (Pubitemid 351766604)
    • (2008) Developmental Cell , vol.14 , Issue.6 , pp. 902-913
    • Im, Y.J.1    Hurley, J.H.2
  • 19
    • 68449095867 scopus 로고    scopus 로고
    • Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis
    • Y.J. Im, T. Wollert, E. Boura, and J.H. Hurley Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis Dev. Cell 17 2009 234 243
    • (2009) Dev. Cell , vol.17 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3    Hurley, J.H.4
  • 23
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • DOI 10.1016/S0092-8674(01)00434-2
    • D.J. Katzmann, M. Babst, and S.D. Emr Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I Cell 106 2001 145 155 (Pubitemid 32772626)
    • (2001) Cell , vol.106 , Issue.2 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 24
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • DOI 10.1083/jcb.200302136
    • D.J. Katzmann, C.J. Stefan, M. Babst, and S.D. Emr Vps27 recruits ESCRT machinery to endosomes during MVB sorting J. Cell Biol. 162 2003 413 423 (Pubitemid 36988551)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 26
    • 34247634126 scopus 로고    scopus 로고
    • Molecular Architecture and Functional Model of the Complete Yeast ESCRT-I Heterotetramer
    • DOI 10.1016/j.cell.2007.03.016, PII S0092867407003790
    • M.S. Kostelansky, C. Schluter, Y.Y.C. Tam, S. Lee, R. Ghirlando, B. Beach, E. Conibear, and J.H. Hurley Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer Cell 129 2007 485 498 (Pubitemid 46671555)
    • (2007) Cell , vol.129 , Issue.3 , pp. 485-498
    • Kostelansky, M.S.1    Schluter, C.2    Tam, Y.Y.C.3    Lee, S.4    Ghirlando, R.5    Beach, B.6    Conibear, E.7    Hurley, J.H.8
  • 30
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • DOI 10.1083/jcb.200401141
    • J. McCullough, M.J. Clague, and S. Urbé AMSH is an endosome-associated ubiquitin isopeptidase J. Cell Biol. 166 2004 487 492 (Pubitemid 39097168)
    • (2004) Journal of Cell Biology , vol.166 , Issue.4 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 32
    • 12044255574 scopus 로고
    • Fluctuating vesicles of nonspherical topology
    • X. Michalet, D. Bensimon, and B. Fourcade Fluctuating vesicles of nonspherical topology Phys. Rev. Lett. 72 1994 168 171 (Pubitemid 24974937)
    • (1994) Physical Review Letters , vol.72 , Issue.1 , pp. 168-171
    • Michalet, X.1    Bensimon, D.2    Fourcade, B.3
  • 34
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 35
    • 1442317538 scopus 로고    scopus 로고
    • BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
    • DOI 10.1126/science.1092586
    • B.J. Peter, H.M. Kent, I.G. Mills, Y. Vallis, P.J.G. Butler, P.R. Evans, and H.T. McMahon BAR domains as sensors of membrane curvature: the amphiphysin BAR structure Science 303 2004 495 499 (Pubitemid 38120842)
    • (2004) Science , vol.303 , Issue.5657 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6    McMahon, H.T.7
  • 36
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Y. Polyhach, E. Bordignon, and G. Jeschke Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2011 2356 2366
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 38
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • C. Raiborg, and H. Stenmark The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins Nature 458 2009 445 452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 40
    • 85027934034 scopus 로고    scopus 로고
    • Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast
    • X. Ren, and J.H. Hurley Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast EMBO J. 30 2011 2130 2139
    • (2011) EMBO J. , vol.30 , pp. 2130-2139
    • Ren, X.1    Hurley, J.H.2
  • 41
    • 34249073136 scopus 로고    scopus 로고
    • Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies
    • DOI 10.1038/sj.emboj.7601692, PII 7601692
    • C. Richter, M. West, and G. Odorizzi Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies EMBO J. 26 2007 2454 2464 (Pubitemid 46788318)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2454-2464
    • Richter, C.1    West, M.2    Odorizzi, G.3
  • 42
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • B. Różycki, Y.C. Kim, and G. Hummer SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions Structure 19 2011 109 116
    • (2011) Structure , vol.19 , pp. 109-116
    • Rózycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 43
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • DOI 10.1091/mbc.01-10-0525
    • M. Sachse, S. Urbé, V. Oorschot, G.J. Strous, and J. Klumperman Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes Mol. Biol. Cell 13 2002 1313 1328 (Pubitemid 34309625)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1313-1328
    • Sachse, M.1    Urbe, S.2    Oorschot, V.3    Strous, G.J.4    Klumperman, J.5
  • 46
    • 77953893804 scopus 로고    scopus 로고
    • The nuclear pore complex: Bridging nuclear transport and gene regulation
    • C. Strambio-De-Castillia, M. Niepel, and M.P. Rout The nuclear pore complex: bridging nuclear transport and gene regulation Nat. Rev. Mol. Cell Biol. 11 2010 490 501
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 490-501
    • Strambio-De-Castillia, C.1    Niepel, M.2    Rout, M.P.3
  • 47
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • DOI 10.1006/prep.2000.1363
    • S. Tan A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli Protein Expr. Purif. 21 2001 224 234 (Pubitemid 32614518)
    • (2001) Protein Expression and Purification , vol.21 , Issue.1 , pp. 224-234
    • Tan, S.1
  • 48
    • 77649335931 scopus 로고    scopus 로고
    • ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation
    • D. Teis, S. Saksena, B.L. Judson, and S.D. Emr ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation EMBO J. 29 2010 871 883
    • (2010) EMBO J. , vol.29 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3    Emr, S.D.4
  • 49
    • 5044245523 scopus 로고    scopus 로고
    • ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes
    • DOI 10.1016/j.devcel.2004.09.003, PII S1534580704003235
    • H. Teo, O. Perisic, B. González, and R.L. Williams ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes Dev. Cell 7 2004 559 569 (Pubitemid 39341841)
    • (2004) Developmental Cell , vol.7 , Issue.4 , pp. 559-569
    • Teo, H.1    Perisic, O.2    Gonzalez, B.3    Williams, R.L.4
  • 50
    • 3142581995 scopus 로고    scopus 로고
    • Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins
    • DOI 10.1074/jbc.M400023200
    • H. Teo, D.B. Veprintsev, and R.L. Williams Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins J. Biol. Chem. 279 2004 28689 28696 (Pubitemid 38900153)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28689-28696
    • Teo, H.1    Veprintsev, D.B.2    Williams, R.L.3
  • 51
    • 33645981584 scopus 로고    scopus 로고
    • ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes
    • H.L. Teo, D.J. Gill, J. Sun, O. Perisic, D.B. Veprintsev, Y. Vallis, S.D. Emr, and R.L. Williams ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes Cell 125 2006 99 111
    • (2006) Cell , vol.125 , pp. 99-111
    • Teo, H.L.1    Gill, D.J.2    Sun, J.3    Perisic, O.4    Veprintsev, D.B.5    Vallis, Y.6    Emr, S.D.7    Williams, R.L.8
  • 52
    • 78951470141 scopus 로고    scopus 로고
    • Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast
    • M. Wemmer, I. Azmi, M. West, B. Davies, D. Katzmann, and G. Odorizzi Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast J. Cell Biol. 192 2011 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
  • 53
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • DOI 10.1038/nrm2162, PII NRM2162
    • R.L. Williams, and S. Urbé The emerging shape of the ESCRT machinery Nat. Rev. Mol. Cell Biol. 8 2007 355 368 (Pubitemid 46643239)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 355-368
    • Williams, R.L.1    Urbe, S.2
  • 54
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • T. Wollert, and J.H. Hurley Molecular mechanism of multivesicular body biogenesis by ESCRT complexes Nature 464 2010 864 869
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 56
    • 77955487325 scopus 로고    scopus 로고
    • Structural role of the Vps4-Vta1 interface in ESCRT-III recycling
    • D. Yang, and J.H. Hurley Structural role of the Vps4-Vta1 interface in ESCRT-III recycling Structure 18 2010 976 984
    • (2010) Structure , vol.18 , pp. 976-984
    • Yang, D.1    Hurley, J.H.2


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