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Volumn 68, Issue , 2011, Pages 33-47

Dynamic Remodeling of Membranes Catalyzed by Dynamin

Author keywords

Dynamin; GTPase; Membrane fission; Membrane tethers; Reconstitution; Supported bilayers

Indexed keywords


EID: 79960423864     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385891-7.00002-7     Document Type: Book
Times cited : (4)

References (46)
  • 1
    • 0037077224 scopus 로고    scopus 로고
    • The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum
    • Accola M.A., Huang B., Al Masri A., McNiven M.A. The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum. Journal of Biological Chemistry 2002, 277(24):21829-21835.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21829-21835
    • Accola, M.A.1    Huang, B.2    Al Masri, A.3    McNiven, M.A.4
  • 2
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
    • Bashkirov P.V., Akimov S.A., Evseev A.I., Schmid S.L., Zimmerberg J., Frolov V.A. GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission. Cell 2008, 135(7):1276-1286.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5    Frolov, V.A.6
  • 5
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo F., McMahon H.T., Kozlov M.M. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophysical Journal 2008, 95(5):2325-2339.
    • (2008) Biophysical Journal , vol.95 , Issue.5 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 6
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie J.S., Acharya S., Leonard M., Schmid S.L., Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 2010, 465(7297):435-440.
    • (2010) Nature , vol.465 , Issue.7297 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 9
    • 4344586301 scopus 로고    scopus 로고
    • Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin
    • Danino D., Moon K.H., Hinshaw J.E. Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin. Journal of Structural Biology 2004, 147(3):259-267.
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 259-267
    • Danino, D.1    Moon, K.H.2    Hinshaw, J.E.3
  • 10
    • 79952280348 scopus 로고    scopus 로고
    • Rapid and efficient clathrin-mediated endocytosis revealed in genome-edited mammalian cells
    • Doyon J.B., Zeitler B., Cheng J., Cheng A.T., Cherone J.M., Santiago Y., et al. Rapid and efficient clathrin-mediated endocytosis revealed in genome-edited mammalian cells. Nature Cell Biology 2011, 13(3):331-337.
    • (2011) Nature Cell Biology , vol.13 , Issue.3 , pp. 331-337
    • Doyon, J.B.1    Zeitler, B.2    Cheng, J.3    Cheng, A.T.4    Cherone, J.M.5    Santiago, Y.6
  • 12
    • 77953028450 scopus 로고    scopus 로고
    • Structural basis of oligomerization in the stalk region of dynamin-like MxA
    • Gao S., von der Malsburg A., Paeschke S., Behlke J., Haller O., Kochs G., et al. Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature 2010, 465(7297):502-506.
    • (2010) Nature , vol.465 , Issue.7297 , pp. 502-506
    • Gao, S.1    von der Malsburg, A.2    Paeschke, S.3    Behlke, J.4    Haller, O.5    Kochs, G.6
  • 13
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J.E., Schmid S.L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 1995, 374(6518):190-192.
    • (1995) Nature , vol.374 , Issue.6518 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 14
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Developmental Cell 2005, 9(6):791-804.
    • (2005) Developmental Cell , vol.9 , Issue.6 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 16
    • 0036469355 scopus 로고    scopus 로고
    • The dynamin A ring complex: Molecular organization and nucleotide-dependent conformational changes
    • Klockow B., Tichelaar W., Madden D.R., Niemann H.H., Akiba T., Hirose K., et al. The dynamin A ring complex: Molecular organization and nucleotide-dependent conformational changes. EMBO Journal 2002, 21(3):240-250.
    • (2002) EMBO Journal , vol.21 , Issue.3 , pp. 240-250
    • Klockow, B.1    Tichelaar, W.2    Madden, D.R.3    Niemann, H.H.4    Akiba, T.5    Hirose, K.6
  • 17
    • 0021039168 scopus 로고
    • Evidence for a presynaptic blockage of transmission in a temperature-sensitive mutant of Drosophila
    • Koenig J.H., Ikeda K. Evidence for a presynaptic blockage of transmission in a temperature-sensitive mutant of Drosophila. Journal of Neurobiology 1983, 14(6):411-419.
    • (1983) Journal of Neurobiology , vol.14 , Issue.6 , pp. 411-419
    • Koenig, J.H.1    Ikeda, K.2
  • 18
    • 33845672530 scopus 로고    scopus 로고
    • A bacterial dynamin-like protein
    • Low H.H., Lowe J. A bacterial dynamin-like protein. Nature 2006, 444(7120):766-769.
    • (2006) Nature , vol.444 , Issue.7120 , pp. 766-769
    • Low, H.H.1    Lowe, J.2
  • 19
    • 78649655812 scopus 로고    scopus 로고
    • Dynamin architecture-From monomer to polymer
    • Low H.H., Lowe J. Dynamin architecture-From monomer to polymer. Current Opinion in Structural Biology 2010, 20(6):791-798.
    • (2010) Current Opinion in Structural Biology , vol.20 , Issue.6 , pp. 791-798
    • Low, H.H.1    Lowe, J.2
  • 20
    • 72249102216 scopus 로고    scopus 로고
    • Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving
    • Low H.H., Sachse C., Amos L.A., Lowe J. Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell 2009, 139(7):1342-1352.
    • (2009) Cell , vol.139 , Issue.7 , pp. 1342-1352
    • Low, H.H.1    Sachse, C.2    Amos, L.A.3    Lowe, J.4
  • 21
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • Marks B., Stowell M.H., Vallis Y., Mills I.G., Gibson A., Hopkins C.R., et al. GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 2001, 410(6825):231-235.
    • (2001) Nature , vol.410 , Issue.6825 , pp. 231-235
    • Marks, B.1    Stowell, M.H.2    Vallis, Y.3    Mills, I.G.4    Gibson, A.5    Hopkins, C.R.6
  • 22
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 2005, 438(7068):590-596.
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 23
    • 35148862219 scopus 로고    scopus 로고
    • A corkscrew model for dynamin constriction
    • Mears J.A., Ray P., Hinshaw J.E. A corkscrew model for dynamin constriction. Structure 2007, 15(10):1190-1202.
    • (2007) Structure , vol.15 , Issue.10 , pp. 1190-1202
    • Mears, J.A.1    Ray, P.2    Hinshaw, J.E.3
  • 24
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • Merrifield C.J., Perrais D., Zenisek D. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 2005, 121(4):593-606.
    • (2005) Cell , vol.121 , Issue.4 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 25
    • 0030967213 scopus 로고    scopus 로고
    • Role of the basic, proline-rich region of dynamin in Src homology 3 domain binding and endocytosis
    • Okamoto P.M., Herskovits J.S., Vallee R.B. Role of the basic, proline-rich region of dynamin in Src homology 3 domain binding and endocytosis. Journal of Biological Chemistry 1997, 272(17):11629-11635.
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11629-11635
    • Okamoto, P.M.1    Herskovits, J.S.2    Vallee, R.B.3
  • 26
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: Universal membrane tubulation and fission molecules?. Nature Reviews Molecular Cell Biology 2004, 5(2):133-147.
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.2 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 27
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • Pucadyil T.J., Schmid S.L. Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell 2008, 135(7):1263-1275.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 28
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions of membrane active GTPases in coated vesicle formation
    • Pucadyil T.J., Schmid S.L. Conserved functions of membrane active GTPases in coated vesicle formation. Science 2009, 325(5945):1217-1220.
    • (2009) Science , vol.325 , Issue.5945 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 29
    • 77955152146 scopus 로고    scopus 로고
    • Supported bilayers with excess membrane reservoir: A template for reconstituting membrane budding and fission
    • Pucadyil T.J., Schmid S.L. Supported bilayers with excess membrane reservoir: A template for reconstituting membrane budding and fission. Biophysical Journal 2010, 99(2):517-525.
    • (2010) Biophysical Journal , vol.99 , Issue.2 , pp. 517-525
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 30
    • 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 T.J., Liu Y.W., Acharya S., Leonard M., Lukiyanchuk V., et al. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Molecular Biology of the Cell 2009, 20(22):4630-4639.
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.22 , pp. 4630-4639
    • Ramachandran, R.1    Pucadyil, T.J.2    Liu, Y.W.3    Acharya, S.4    Leonard, M.5    Lukiyanchuk, V.6
  • 31
    • 38049052532 scopus 로고    scopus 로고
    • Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane
    • Ramachandran R., Schmid S.L. Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane. EMBO Journal 2008, 27(1):27-37.
    • (2008) EMBO Journal , vol.27 , Issue.1 , pp. 27-37
    • Ramachandran, R.1    Schmid, S.L.2
  • 33
    • 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. GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 2006, 441(7092):528-531.
    • (2006) Nature , vol.441 , Issue.7092 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 34
    • 0034189032 scopus 로고    scopus 로고
    • Garrotes, springs, ratchets, and whips: Putting dynamin models to the test
    • Sever S., Damke H., Schmid S.L. Garrotes, springs, ratchets, and whips: Putting dynamin models to the test. Traffic 2000, 1(5):385-392.
    • (2000) Traffic , vol.1 , Issue.5 , pp. 385-392
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 35
    • 0037452537 scopus 로고    scopus 로고
    • A molecular motor or a regulator? Dynamin's in a class of its own
    • Song B.D., Schmid S.L. A molecular motor or a regulator? Dynamin's in a class of its own. Biochemistry 2003, 42(6):1369-1376.
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1369-1376
    • Song, B.D.1    Schmid, S.L.2
  • 36
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell M.H., Marks B., Wigge P., McMahon H.T. Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring. Nature Cell Biology 1999, 1(1):27-32.
    • (1999) Nature Cell Biology , vol.1 , Issue.1 , pp. 27-32
    • Stowell, M.H.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 37
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck D.K., Hoekstra D., Pagano R.E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 1981, 20(14):4093-4099.
    • (1981) Biochemistry , vol.20 , Issue.14 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 38
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S.M., Hinshaw J.E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 1998, 93(6):1021-1029.
    • (1998) Cell , vol.93 , Issue.6 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 39
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 1995, 374(6518):186-190.
    • (1995) Nature , vol.374 , Issue.6518 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 40
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: Selecting cargo for clathrin-regulated internalization
    • Traub L.M. Tickets to ride: Selecting cargo for clathrin-regulated internalization. Nature Reviews Molecular Cell Biology 2009, 10(9):583-596.
    • (2009) Nature Reviews Molecular Cell Biology , vol.10 , Issue.9 , pp. 583-596
    • Traub, L.M.1
  • 41
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
    • van der Bliek A.M., Meyerowitz E.M. Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic. Nature 1991, 351(6325):411-414.
    • (1991) Nature , vol.351 , Issue.6325 , pp. 411-414
    • van der Bliek, A.M.1    Meyerowitz, E.M.2
  • 43
    • 0018653707 scopus 로고
    • 2+-induced fusion of phospholipid vesicles monitored by mixing of aqueous contents
    • 2+-induced fusion of phospholipid vesicles monitored by mixing of aqueous contents. Nature 1979, 281(5733):690-692.
    • (1979) Nature , vol.281 , Issue.5733 , pp. 690-692
    • Wilschut, J.1    Papahadjopoulos, D.2
  • 44
    • 79960433719 scopus 로고    scopus 로고
    • Crystal structure of the dynamin 3 GTPase domain bound with GDP. PDB3L43.
    • Yang, S., Tempel, W., Tong, Y., Nedyalkova, L., Guan, X., Crombet, L., et al. (2009). Crystal structure of the dynamin 3 GTPase domain bound with GDP. PDB3L43.
    • (2009)
    • Yang, S.1    Tempel, W.2    Tong, Y.3    Nedyalkova, L.4    Guan, X.5    Crombet, L.6
  • 45
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar D., Waterman-Storer C.M., Schmid S.L. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Molecular Biology of the Cell 2005, 16(2):964-975.
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.2 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 46
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P., Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nature Cell Biology 2001, 3(10):922-926.
    • (2001) Nature Cell Biology , vol.3 , Issue.10 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.