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Volumn 8, Issue 1, 2013, Pages

Dynamin-Catalyzed Membrane Fission Requires Coordinated GTP Hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; DYNAMIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN;

EID: 84873208803     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055691     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 53149101681 scopus 로고    scopus 로고
    • Correlation between self-association modes and GTPase activation of dynamin
    • Binns DD, Barylko B, Grichine N, Adkinson AL, Helms MK, et al. (1999) Correlation between self-association modes and GTPase activation of dynamin. J Protein Chem 18: 277-290.
    • (1999) J Protein Chem , vol.18 , pp. 277-290
    • Binns, D.D.1    Barylko, B.2    Grichine, N.3    Adkinson, A.L.4    Helms, M.K.5
  • 2
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring
    • Stowell MHB, Marks B, Wigge P, McMahon HT, (1999) Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat Cell Biol 1: 27-32.
    • (1999) Nat Cell Biol , vol.1 , pp. 27-32
    • Stowell, M.H.B.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 3
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self assembly stimulates its GTPase activity
    • Warnock DE, Hinshaw JE, Schmid SL, (1996) Dynamin self assembly stimulates its GTPase activity. J Biol Chem 271: 22310-22314.
    • (1996) J Biol Chem , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 4
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • Ehrlich M, Boll W, Van Oijen A, Hariharan R, Chandran K, et al. (2004) Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell 118: 591-605.
    • (2004) Cell , vol.118 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5
  • 5
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield C, Feldman ME, Wan L, Almers W, (2002) Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat Cell Biol 4: 691-698.
    • (2002) Nat Cell Biol , vol.4 , pp. 691-698
    • Merrifield, C.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 6
    • 84859986511 scopus 로고    scopus 로고
    • A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis
    • Taylor MJ, Lampe M, Merrifield CJ, (2012) A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis. PLoS Biol 10: e1001302.
    • (2012) PLoS Biol , vol.10
    • Taylor, M.J.1    Lampe, M.2    Merrifield, C.J.3
  • 9
    • 0034605101 scopus 로고    scopus 로고
    • Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis
    • Sever S, Damke H, Schmid SL, (2000) Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis. J Cell Biol 150: 1137-1148.
    • (2000) J Cell Biol , vol.150 , pp. 1137-1148
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 11
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke GJK, McMahon HT, (2004) The dynamin superfamily: Universal membrane tubulation and fission molecules? Nature Rev Mol Cell Biol 5: 133-147.
    • (2004) Nature Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.K.1    McMahon, H.T.2
  • 12
    • 80052248915 scopus 로고    scopus 로고
    • Dynamin: functional design of a membrane fission catalyst
    • Schmid SL, Frolov VA, (2011) Dynamin: functional design of a membrane fission catalyst. Annu Rev Cell Dev Biol 27: 79-105.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 79-105
    • Schmid, S.L.1    Frolov, V.A.2
  • 13
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, Schmid SL, (1994) Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Cell Biol 127: 915-934.
    • (1994) J Cell Biol , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 15
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • Marks B, Stowell MHB, Vallis Y, Mills IG, Gibson A, et al. (2001) GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 410: 231-235.
    • (2001) Nature , vol.410 , pp. 231-235
    • Marks, B.1    Stowell, M.H.B.2    Vallis, Y.3    Mills, I.G.4    Gibson, A.5
  • 16
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F, (2010) G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 465: 435-440.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 17
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis
    • Achiriloaie M, Barylko B, Albanesi JP, (1999) Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol Cell Biol 19: 1410-1415.
    • (1999) Mol Cell Biol , vol.19 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 18
    • 0033545702 scopus 로고    scopus 로고
    • Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
    • Lee A, Frank DW, Marks MS, Lemmon MA, (1999) Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Curr Biol 9: 261-264.
    • (1999) Curr Biol , vol.9 , pp. 261-264
    • Lee, A.1    Frank, D.W.2    Marks, M.S.3    Lemmon, M.A.4
  • 19
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin- mediated endocytosis
    • Vallis Y, Wigge P, Marks B, Evans PR, McMahon HT, (1999) Importance of the pleckstrin homology domain of dynamin in clathrin- mediated endocytosis. Curr Biol 9: 257-260.
    • (1999) Curr Biol , vol.9 , pp. 257-260
    • Vallis, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 20
    • 33846513580 scopus 로고    scopus 로고
    • The dynamin middle domain is critical for tetramerization and higher-order self-assembly
    • Ramachandran R, Surka M, Chappie JS, Fowler DM, Foss TR, et al. (2007) The dynamin middle domain is critical for tetramerization and higher-order self-assembly. Embo J 26: 559-566.
    • (2007) Embo J , vol.26 , pp. 559-566
    • Ramachandran, R.1    Surka, M.2    Chappie, J.S.3    Fowler, D.M.4    Foss, T.R.5
  • 21
    • 2342473321 scopus 로고    scopus 로고
    • An assembly-incompetent mutant establishes a requirement for dynamin in self-assembly in clathrin-mediated endocytosis in vivo
    • Song BD, Yarar D, Schmid SL, (2004a) An assembly-incompetent mutant establishes a requirement for dynamin in self-assembly in clathrin-mediated endocytosis in vivo. Mol Biol Cell 15: 2243-2252.
    • (2004) Mol Biol Cell , vol.15 , pp. 2243-2252
    • Song, B.D.1    Yarar, D.2    Schmid, S.L.3
  • 22
    • 73949099250 scopus 로고    scopus 로고
    • Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission
    • Ramachandran R, Pucadyil TJ, Liu YW, Acharya S, Leonard M, et al. (2009) Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol Biol Cell 20: 4630-4639.
    • (2009) Mol Biol Cell , vol.20 , pp. 4630-4639
    • Ramachandran, R.1    Pucadyil, T.J.2    Liu, Y.W.3    Acharya, S.4    Leonard, M.5
  • 23
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon HT, Boucrot E, (2011) Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 12: 517-533.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 24
    • 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
  • 25
    • 77955152146 scopus 로고    scopus 로고
    • Supported Bilayers With Excess Membrane Reservoir: A Template For Reconstituting Membrane Budding and Fission
    • Pucadyil TJ, Schmid SL, (2010) Supported Bilayers With Excess Membrane Reservoir: A Template For Reconstituting Membrane Budding and Fission. Biophys J 99: 517-525.
    • (2010) Biophys J , vol.99 , pp. 517-525
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 26
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever S, Muhlberg AB, Schmid SL, (1999) Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature 398: 481-486.
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 27
    • 84867388584 scopus 로고    scopus 로고
    • Structural insights into dynamin-mediated membrane fission
    • Faelber K, Held M, Gao S, Posor Y, Haucke V, et al. (2012) Structural insights into dynamin-mediated membrane fission. Structure 20: 1621-1628.
    • (2012) Structure , vol.20 , pp. 1621-1628
    • Faelber, K.1    Held, M.2    Gao, S.3    Posor, Y.4    Haucke, V.5
  • 28
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • Ford MG, Jenni S, Nunnari J, (2011) The crystal structure of dynamin. Nature 477: 561-566.
    • (2011) Nature , vol.477 , pp. 561-566
    • Ford, M.G.1    Jenni, S.2    Nunnari, J.3
  • 29
    • 80053501669 scopus 로고    scopus 로고
    • Structural insights into the assembly of a fission machine
    • Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, et al. (2011) Structural insights into the assembly of a fission machine. Cell 147: 209-222.
    • (2011) Cell , vol.147 , pp. 209-222
    • Chappie, J.S.1    Mears, J.A.2    Fang, S.3    Leonard, M.4    Schmid, S.L.5
  • 30
    • 4644314874 scopus 로고    scopus 로고
    • Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis
    • Song BD, Leonard M, Schmid SL, (2004b) Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis. J Biol Chem 279: 40431-40436.
    • (2004) J Biol Chem , vol.279 , pp. 40431-40436
    • Song, B.D.1    Leonard, M.2    Schmid, S.L.3
  • 31
    • 84859175662 scopus 로고    scopus 로고
    • Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains
    • Boucrot E, Pick A, Camdere G, Liska N, Evergren E, et al. (2012) Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains. Cell 149: 124-136.
    • (2012) Cell , vol.149 , pp. 124-136
    • Boucrot, E.1    Pick, A.2    Camdere, G.3    Liska, N.4    Evergren, E.5
  • 32
    • 0034691319 scopus 로고    scopus 로고
    • The mechanism of GTP hydrolysis by dynamin II: a transient kinetic study
    • Binns DD, Helms MK, Barylko B, Davis CT, Jameson DM, et al. (2000) The mechanism of GTP hydrolysis by dynamin II: a transient kinetic study. Biochemistry 39: 7188-7196.
    • (2000) Biochemistry , vol.39 , pp. 7188-7196
    • Binns, D.D.1    Helms, M.K.2    Barylko, B.3    Davis, C.T.4    Jameson, D.M.5
  • 33
    • 17644424000 scopus 로고    scopus 로고
    • An internal GAP domain negatively regulates presynaptic dynamin in vivo: A two-step model of dynamin function
    • Narayanan R, Leonard M, Song BD, Schmid SL, Ramaswami M, (2005) An internal GAP domain negatively regulates presynaptic dynamin in vivo: A two-step model of dynamin function. J Cell Biol 169: 117-126.
    • (2005) J Cell Biol , vol.169 , pp. 117-126
    • Narayanan, R.1    Leonard, M.2    Song, B.D.3    Schmid, S.L.4    Ramaswami, M.5
  • 34
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut TW, (1994) Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 140: 1-22.
    • (1994) Mol Cell Biochem , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 35
    • 0035162334 scopus 로고    scopus 로고
    • Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages
    • Damke H, Binns DD, Ueda H, Schmid SL, Baba T, (2001) Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages. Mol Biol Cell 12: 2578-2589.
    • (2001) Mol Biol Cell , vol.12 , pp. 2578-2589
    • Damke, H.1    Binns, D.D.2    Ueda, H.3    Schmid, S.L.4    Baba, T.5
  • 36
    • 68149110312 scopus 로고    scopus 로고
    • An intramolecular signaling element that modulates dynamin function in vitro and in vivo
    • Chappie JS, Acharya S, Liu YW, Leonard M, Pucadyil TJ, et al. (2009) An intramolecular signaling element that modulates dynamin function in vitro and in vivo. Mol Biol Cell 20: 3561-3571.
    • (2009) Mol Biol Cell , vol.20 , pp. 3561-3571
    • Chappie, J.S.1    Acharya, S.2    Liu, Y.W.3    Leonard, M.4    Pucadyil, T.J.5
  • 38
    • 71649086146 scopus 로고    scopus 로고
    • Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits
    • Ferguson S, Raimondi A, Paradise S, Shen H, Mesaki K, et al. (2009) Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits. Dev Cell 17: 811-822.
    • (2009) Dev Cell , vol.17 , pp. 811-822
    • Ferguson, S.1    Raimondi, A.2    Paradise, S.3    Shen, H.4    Mesaki, K.5
  • 39
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P, Hinshaw JE, (2001) Three-dimensional reconstruction of dynamin in the constricted state. Nat Cell Biol 3: 922-926.
    • (2001) Nat Cell Biol , vol.3 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2
  • 40
    • 80053501669 scopus 로고    scopus 로고
    • A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke
    • Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, et al. (2011) A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke. Cell 147: 209-222.
    • (2011) Cell , vol.147 , pp. 209-222
    • Chappie, J.S.1    Mears, J.A.2    Fang, S.3    Leonard, M.4    Schmid, S.L.5
  • 41
    • 0024368508 scopus 로고
    • Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval
    • Koenig JH, Ikeda K, (1989) Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval. J Neuroscience 9: 3844-3860.
    • (1989) J Neuroscience , vol.9 , pp. 3844-3860
    • Koenig, J.H.1    Ikeda, K.2
  • 42
    • 79951831654 scopus 로고    scopus 로고
    • Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin
    • Shen H, Ferguson SM, Dephoure N, Park R, Yang Y, et al. (2011) Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin. Mol Biol Cell 22: 493-502.
    • (2011) Mol Biol Cell , vol.22 , pp. 493-502
    • Shen, H.1    Ferguson, S.M.2    Dephoure, N.3    Park, R.4    Yang, Y.5
  • 43
    • 30544447100 scopus 로고    scopus 로고
    • Robust colorimetric assays for dynamin's basal and stimulated GTPase activities
    • Leonard M, Song BD, Ramachandran R, Schmid SL, (2005) Robust colorimetric assays for dynamin's basal and stimulated GTPase activities. Methods Enzymol 404: 490-503.
    • (2005) Methods Enzymol , vol.404 , pp. 490-503
    • Leonard, M.1    Song, B.D.2    Ramachandran, R.3    Schmid, S.L.4
  • 44
    • 0035971163 scopus 로고    scopus 로고
    • Receptor and membrane recycling can occur with unaltered efficiency despite dramatic Rab5(q79l)-induced changes in endosome geometry
    • Ceresa BP, Lotscher M, Schmid SL, (2001) Receptor and membrane recycling can occur with unaltered efficiency despite dramatic Rab5(q79l)-induced changes in endosome geometry. J Biol Chem 276: 9649-9654.
    • (2001) J Biol Chem , vol.276 , pp. 9649-9654
    • Ceresa, B.P.1    Lotscher, M.2    Schmid, S.L.3
  • 45
    • 59449088311 scopus 로고    scopus 로고
    • Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells
    • Liu YW, Surka MC, Schroeter T, Lukiyanchuk V, Schmid SL, (2008) Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells. Mol Biol Cell 19: 5347-5359.
    • (2008) Mol Biol Cell , vol.19 , pp. 5347-5359
    • Liu, Y.W.1    Surka, M.C.2    Schroeter, T.3    Lukiyanchuk, V.4    Schmid, S.L.5


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