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Volumn 129, Issue 4, 2007, Pages 761-772

Curved EFC/F-BAR-Domain Dimers Are Joined End to End into a Filament for Membrane Invagination in Endocytosis

Author keywords

CELLBIO; PROTEINS

Indexed keywords

CDC42 INTERACTING PROTEIN 4; CLATHRIN; DIMER; FORMIN BINDING PROTEIN 17; PROTEIN; UNCLASSIFIED DRUG;

EID: 34249316521     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.03.040     Document Type: Article
Times cited : (352)

References (49)
  • 1
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton
    • Aspenström P. A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr. Biol. 7 (1997) 479-487
    • (1997) Curr. Biol. , vol.7 , pp. 479-487
    • Aspenström, P.1
  • 3
    • 0028103275 scopus 로고
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 4
    • 2542480756 scopus 로고    scopus 로고
    • The stalk region of dynamin drives the constriction of dynamin tubes
    • Chen Y.J., Zhang P., Egelman E.H., and Hinshaw J.E. The stalk region of dynamin drives the constriction of dynamin tubes. Nat. Struct. Mol. Biol. 11 (2004) 574-575
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 574-575
    • Chen, Y.J.1    Zhang, P.2    Egelman, E.H.3    Hinshaw, J.E.4
  • 5
    • 0034903709 scopus 로고    scopus 로고
    • Transmission electron microscopy with Zernike phase plate
    • Danev R., and Nagayama K. Transmission electron microscopy with Zernike phase plate. Ultramicroscopy 88 (2001) 243-252
    • (2001) Ultramicroscopy , vol.88 , pp. 243-252
    • Danev, R.1    Nagayama, K.2
  • 6
    • 33748964289 scopus 로고    scopus 로고
    • Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis
    • Dawson J.C., Legg J.A., and Machesky L.M. Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis. Trends Cell Biol. 16 (2006) 493-498
    • (2006) Trends Cell Biol. , vol.16 , pp. 493-498
    • Dawson, J.C.1    Legg, J.A.2    Machesky, L.M.3
  • 11
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J.E., and Schmid S.L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374 (1995) 190-192
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 12
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho H.Y., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P., and Kirschner M.W. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118 (2004) 203-216
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Ma, L.4    Li, J.5    Gygi, S.P.6    Kirschner, M.W.7
  • 13
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77 (1989) 61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 14
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T., and De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 1761 (2006) 897-912
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 15
    • 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., and De Camilli P. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 9 (2005) 791-804
    • (2005) Dev. Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen M., Toret C.P., and Drubin D.G. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123 (2005) 305-320
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 18
  • 19
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M., and Mochizuki N. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J. Biol. Chem. 279 (2004) 40091-40099
    • (2004) J. Biol. Chem. , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4    Masuda, M.5    Matsuda, M.6    Mochizuki, N.7
  • 20
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: linking membrane trafficking with the cytoskeleton
    • Kessels M.M., and Qualmann B. The syndapin protein family: linking membrane trafficking with the cytoskeleton. J. Cell Sci. 117 (2004) 3077-3086
    • (2004) J. Cell Sci. , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 21
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., and Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442 (1999) 15-19
    • (1999) FEBS Lett. , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 23
    • 0026244229 scopus 로고
    • MolScript-a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MolScript-a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 24
    • 0034656215 scopus 로고    scopus 로고
    • Involvement of PCH family proteins in cytokinesis and actin distribution
    • Lippincott J., and Li R. Involvement of PCH family proteins in cytokinesis and actin distribution. Microsc. Res. Tech. 49 (2000) 168-172
    • (2000) Microsc. Res. Tech. , vol.49 , pp. 168-172
    • Lippincott, J.1    Li, R.2
  • 25
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • Masuda M., Takeda S., Sone M., Ohki T., Mori H., Kamioka Y., and Mochizuki N. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 25 (2006) 2889-2897
    • (2006) EMBO J. , vol.25 , pp. 2889-2897
    • Masuda, M.1    Takeda, S.2    Sone, M.3    Ohki, T.4    Mori, H.5    Kamioka, Y.6    Mochizuki, N.7
  • 26
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanism of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanism of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 27
    • 1842419430 scopus 로고    scopus 로고
    • Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts
    • Merrifield C.J., Qualmann B., Kessels M.M., and Almers W. Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts. Eur. J. Cell Biol. 83 (2004) 13-18
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 13-18
    • Merrifield, C.J.1    Qualmann, B.2    Kessels, M.M.3    Almers, W.4
  • 28
    • 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., and Zenisek D. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121 (2005) 593-606
    • (2005) Cell , vol.121 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 29
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., and Murphy M.E.P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50 (1994) 869-873
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 30
    • 0142026447 scopus 로고    scopus 로고
    • Regulation of actin dynamics by WASP family proteins
    • Miki H., and Takenawa T. Regulation of actin dynamics by WASP family proteins. J. Biochem. (Tokyo) 134 (2003) 309-313
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 309-313
    • Miki, H.1    Takenawa, T.2
  • 31
  • 32
    • 27744518154 scopus 로고    scopus 로고
    • Phase contrast enhancement with phase plates in electron microscopy
    • Nagayama K. Phase contrast enhancement with phase plates in electron microscopy. Ad. Imaging Elec. Phys. 138 (2005) 69-146
    • (2005) Ad. Imaging Elec. Phys. , vol.138 , pp. 69-146
    • Nagayama, K.1
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 27644592393 scopus 로고    scopus 로고
    • Dynamics of endocytic vesicle creation
    • Perrais D., and Merrifield C.J. Dynamics of endocytic vesicle creation. Dev. Cell 9 (2005) 581-592
    • (2005) Dev. Cell , vol.9 , pp. 581-592
    • Perrais, D.1    Merrifield, C.J.2
  • 36
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., and McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 5 (2004) 133-147
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 37
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T., Bell R.E., Mayrose I., Glaser F., and Ben-Tal N. Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18 Suppl 1 (2002) S71-S77
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 39
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A., Uyhazi K., Frost A., and De Camilli P. GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441 (2006) 528-531
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 40
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Schweitzer S.M., and Hinshaw J.E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93 (1998) 1021-1029
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Schweitzer, S.M.1    Hinshaw, J.E.2
  • 44
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., and De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature 374 (1995) 186-190
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 45
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., and De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat. Cell Biol. 1 (1999) 33-39
    • (1999) Nat. Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 46
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
    • Takenawa T., and Suetsugu S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 8 (2007) 37-48
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 47
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., and Takenawa T. Coordination between actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172 (2006) 269-279
    • (2006) J. Cell Biol. , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5    Takenawa, T.6
  • 48
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar D., Waterman-Storer C.M., and Schmid S.L. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol. Biol. Cell 16 (2005) 964-975
    • (2005) Mol. Biol. Cell , vol.16 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 49
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J., and Kozlov M.M. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7 (2006) 9-19
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2


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