메뉴 건너뛰기




Volumn 5, Issue 11, 2009, Pages

Computational model of membrane fission catalyzed by ESCRT-III

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELL PROLIFERATION; COMPUTATION THEORY; COMPUTATIONAL METHODS; DOMES; LIPID BILAYERS; MAMMALS;

EID: 73449092185     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000575     Document Type: Article
Times cited : (133)

References (53)
  • 1
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438: 590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 2
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik LV, Kozlov MM (2003) Protein-lipid interplay in fusion and fission of biological membranes. Annu Rev Biochem 72: 175-207.
    • (2003) Annu Rev Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 4
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J, Kozlov MM (2006) How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 7: 9-19.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 5
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo F, McMahon HT, Kozlov MM (2008) The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys J 95: 2325-2339.
    • (2008) Biophys J , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 6
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE (2000) Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 16: 483-519.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 7
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: Pinching in new places
    • McNiven MA, Cao H, Pitts KR, Yoon Y (2000) The dynamin family of mechanoenzymes: pinching in new places. Trends Biochem Sci 25: 115-120.
    • (2000) Trends Biochem Sci , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 8
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke GJ, McMahon HT (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat Rev Mol Cell Biol 5: 133-147.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 9
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A, Uyhazi K, Frost A, De Camilli P (2006) GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441: 528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 10
    • 0034189032 scopus 로고    scopus 로고
    • Sever S, Damke H, Schmid SL (2000) Garrotes, springs, ratchets, and whips: putting dynamin models to the test. Traffic 1: 385-392.
    • Sever S, Damke H, Schmid SL (2000) Garrotes, springs, ratchets, and whips: putting dynamin models to the test. Traffic 1: 385-392.
  • 11
    • 33644821441 scopus 로고    scopus 로고
    • The multiple activities of CtBP/BARS proteins: The Golgi view
    • Corda D, Colanzi A, Luini A (2006) The multiple activities of CtBP/BARS proteins: the Golgi view. Trends Cell Biol 16: 167-173.
    • (2006) Trends Cell Biol , vol.16 , pp. 167-173
    • Corda, D.1    Colanzi, A.2    Luini, A.3
  • 12
    • 37249016585 scopus 로고    scopus 로고
    • Dimeric PKD regulates membrane fission to form transport carriers at the TGN
    • Bossard C, Bresson D, Polishchuk RS, Malhotra V (2007) Dimeric PKD regulates membrane fission to form transport carriers at the TGN. J Cell Biol 179: 1123-1131.
    • (2007) J Cell Biol , vol.179 , pp. 1123-1131
    • Bossard, C.1    Bresson, D.2    Polishchuk, R.S.3    Malhotra, V.4
  • 13
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S, Hinshaw J (1998) Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93: 1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.1    Hinshaw, J.2
  • 14
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
    • Bashkirov PV, Akimov SA, Evseev AI, Schmid SL, Zimmerberg J, et al. (2008) GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission. Cell 135: 1276-1286.
    • (2008) Cell , vol.135 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5
  • 15
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • Pucadyil TJ, Schmid SL (2008) Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell 135: 1263-1275.
    • (2008) Cell , vol.135 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 17
    • 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
  • 18
    • 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
  • 19
    • 39149132089 scopus 로고    scopus 로고
    • ESCRT complexes and the biogenesis of multivesicular bodies
    • Hurley JH (2008) ESCRT complexes and the biogenesis of multivesicular bodies. Curr Opin Cell Biol 20: 4-11.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 23
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRT machinery in viral budding and cytokinesis
    • McDonald B, Martin-Serrano J (2009) No strings attached: the ESCRT machinery in viral budding and cytokinesis. J Cell Sci 122: 2167-2177.
    • (2009) J Cell Sci , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 24
  • 25
    • 46049099346 scopus 로고    scopus 로고
    • Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding
    • Kieffer C, Skalicky JJ, Morita E, De Domenico I, Ward DM, et al. (2008) Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev Cell 15: 62-73.
    • (2008) Dev Cell , vol.15 , pp. 62-73
    • Kieffer, C.1    Skalicky, J.J.2    Morita, E.3    De Domenico, I.4    Ward, D.M.5
  • 26
    • 0036696804 scopus 로고    scopus 로고
    • ESCRTIII: An endosome-associated heterooligomeric protein complex required for MVB sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD (2002) ESCRTIII: An endosome-associated heterooligomeric protein complex required for MVB sorting. Developmental Cell 3: 271-282.
    • (2002) Developmental 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
  • 27
    • 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
  • 28
    • 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
  • 31
    • 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
  • 32
    • 66749147856 scopus 로고    scopus 로고
    • A crescentshaped ALIX dimer targets escrt-iii chmp4 filaments
    • Pires R, Hartlieb B, Signor L, Schoehn G, Lata S, et al. (2009) A crescentshaped ALIX dimer targets escrt-iii chmp4 filaments. Sructure 17: 843-856.
    • (2009) Sructure , vol.17 , pp. 843-856
    • Pires, R.1    Hartlieb, B.2    Signor, L.3    Schoehn, G.4    Lata, S.5
  • 34
    • 51149106799 scopus 로고    scopus 로고
    • Helical structures of ESCRT-III are disassembled by VPS4
    • Lata S, Schoehn G, Jain A, Pires R, Piehler J, et al. (2008) Helical structures of ESCRT-III are disassembled by VPS4. Science 321: 1354-1357.
    • (2008) Science , vol.321 , pp. 1354-1357
    • Lata, S.1    Schoehn, G.2    Jain, A.3    Pires, R.4    Piehler, J.5
  • 35
    • 0037974484 scopus 로고    scopus 로고
    • Membrane fission: Model for intermediate structures
    • Kozlovsky Y, Kozlov MM (2003) Membrane fission: model for intermediate structures. Biophys J 85: 85-96.
    • (2003) Biophys J , vol.85 , pp. 85-96
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 36
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik LV, Kozlov MM (2005) Membrane hemifusion: crossing a chasm in two leaps. Cell 123: 375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 39
    • 43249126878 scopus 로고    scopus 로고
    • Asymmetric tethering of flat and curved lipid membranes by a golgin
    • Drin G, Morello V, Casella JF, Gounon P, Antonny B (2008) Asymmetric tethering of flat and curved lipid membranes by a golgin. Science 320: 670-673.
    • (2008) Science , vol.320 , pp. 670-673
    • Drin, G.1    Morello, V.2    Casella, J.F.3    Gounon, P.4    Antonny, B.5
  • 40
    • 40049086567 scopus 로고    scopus 로고
    • Structural basis of membrane invagination by F-BAR domains
    • Frost A, Perera R, Roux A, Spasov K, Destaing O, et al. (2008) Structural basis of membrane invagination by F-BAR domains. Cell 132: 807-817.
    • (2008) Cell , vol.132 , pp. 807-817
    • Frost, A.1    Perera, R.2    Roux, A.3    Spasov, K.4    Destaing, O.5
  • 42
    • 84943997802 scopus 로고
    • Elastic Properties of Lipid Bilayers: Theory and Possible Experiments
    • Helfrich W (1973) Elastic Properties of Lipid Bilayers: Theory and Possible Experiments. Z Naturforsch 28c: 693-703.
    • (1973) Z Naturforsch , vol.28 c , pp. 693-703
    • Helfrich, W.1
  • 43
    • 73449090431 scopus 로고    scopus 로고
    • Helfrich W (1990) Elasticity and thermal undulations of fluid films of amphiphiles. In: Charvolin J, Joanny J-F, Zinn-Justin J, eds (1990) Les Houches, 1988 - Liquids and interfaces. pp 212-237.
    • Helfrich W (1990) Elasticity and thermal undulations of fluid films of amphiphiles. In: Charvolin J, Joanny J-F, Zinn-Justin J, eds (1990) Les Houches, 1988 - Liquids and interfaces. pp 212-237.
  • 44
    • 0001153511 scopus 로고
    • The bending rigidity of phosphatidylcholine bilayers. Dependence on experimental methods, sample cell sealing and temperature
    • Niggemann G, Kummrow M, Helfrich W (1995) The bending rigidity of phosphatidylcholine bilayers. Dependence on experimental methods, sample cell sealing and temperature. J Phys II 5: 413-425.
    • (1995) J Phys II , vol.5 , pp. 413-425
    • Niggemann, G.1    Kummrow, M.2    Helfrich, W.3
  • 45
    • 3042776328 scopus 로고    scopus 로고
    • The gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: Relevance to membrane fusion and lipid phase behavior
    • Siegel DP, Kozlov MM (2004) The gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior. Biophys J 87: 366-374.
    • (2004) Biophys J , vol.87 , pp. 366-374
    • Siegel, D.P.1    Kozlov, M.M.2
  • 46
    • 0032302898 scopus 로고    scopus 로고
    • Gaussian curvature modulus of an amphiphilic monolayer
    • Templer RH, Khoo BJ, Seddon JM (1998) Gaussian curvature modulus of an amphiphilic monolayer. Langmuir 14: 7427-7434.
    • (1998) Langmuir , vol.14 , pp. 7427-7434
    • Templer, R.H.1    Khoo, B.J.2    Seddon, J.M.3
  • 50
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • Obita T, Saksena S, Ghazi-Tabatabai S, Gill DJ, Perisic O, et al. (2007) Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449: 735-739.
    • (2007) Nature , vol.449 , pp. 735-739
    • Obita, T.1    Saksena, S.2    Ghazi-Tabatabai, S.3    Gill, D.J.4    Perisic, O.5
  • 51
    • 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
  • 52
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand RP, Parsegian VA (1989) Hydration forces between phospholipid bilayers. Biochim Biophys Acta 988: 351-376.
    • (1989) Biochim Biophys Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 53
    • 33845317263 scopus 로고    scopus 로고
    • Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes 10.1083/jcb.200606113
    • Nickerson DP, West M, Odorizzi G (2006) Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes 10.1083/jcb.200606113. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.