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Volumn 583, Issue 21, 2009, Pages 3401-3404

The direction of actin polymerization for vesicle fission suggested from membranes tubulated by the EFC/F-BAR domain protein FBP17

Author keywords

Actin; Endocytosis; Extended FCH domain; F BAR domain; Neural Wiskott Aldrich syndrome protein; Vesicle movement

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; BIN AMPHIPHYSIN RVS167 DOMAIN PROTEIN; CELL MEMBRANE PROTEIN; CLATHRIN; DYNAMIN; LIPOSOME; MEMBRANE PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROTEIN FBP17; UNCLASSIFIED DRUG;

EID: 70350307197     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.019     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 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
  • 2
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M., Toret C.P., and Drubin D.G. Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 7 (2006) 404-414
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 3
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4, 5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • Rozelle A.L., et al. Phosphatidylinositol 4, 5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10 (2000) 311-320
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1
  • 5
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M., Sun Y., and Drubin D.G. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115 (2003) 475-487
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 7
    • 41549163956 scopus 로고    scopus 로고
    • Taking apart the endocytic machinery
    • Kaksonen M. Taking apart the endocytic machinery. J. Cell Biol. 180 (2008) 1059-1060
    • (2008) J. Cell Biol. , vol.180 , pp. 1059-1060
    • Kaksonen, M.1
  • 10
    • 33845794075 scopus 로고    scopus 로고
    • The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation
    • Suetsugu S., et al. The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. J. Biol. Chem. 281 (2006) 35347-35358
    • (2006) J. Biol. Chem. , vol.281 , pp. 35347-35358
    • Suetsugu, S.1
  • 12
    • 34249316521 scopus 로고    scopus 로고
    • Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis
    • Shimada A., et al. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell 129 (2007) 761-772
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1
  • 13
    • 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
  • 14
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the 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 the 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
  • 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
    • 69249244189 scopus 로고    scopus 로고
    • F-BAR-containing adaptor CIP4 localizes to early endosomes and regulates Epidermal Growth Factor Receptor trafficking and downregulation
    • Hu J., Troglio F., Mukhopadhyay A., Everingham S., Kwok E., Scita G., and Craig A.W. F-BAR-containing adaptor CIP4 localizes to early endosomes and regulates Epidermal Growth Factor Receptor trafficking and downregulation. Cell Signal. 21 (2009) 1686-1697
    • (2009) Cell Signal. , vol.21 , pp. 1686-1697
    • Hu, J.1    Troglio, F.2    Mukhopadhyay, A.3    Everingham, S.4    Kwok, E.5    Scita, G.6    Craig, A.W.7
  • 17
    • 69449092925 scopus 로고    scopus 로고
    • The F-BAR protein CIP4 promotes GLUT4 endocytosis through bidirectional interactions with N-WASp and Dynamin-2
    • Hartig S.M., et al. The F-BAR protein CIP4 promotes GLUT4 endocytosis through bidirectional interactions with N-WASp and Dynamin-2. J. Cell Sci. 122 (2009) 2283-2291
    • (2009) J. Cell Sci. , vol.122 , pp. 2283-2291
    • Hartig, S.M.1
  • 18
    • 39149109271 scopus 로고    scopus 로고
    • IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions
    • Scita G., Confalonieri S., Lappalainen P., and Suetsugu S. IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol. 18 (2008) 52-60
    • (2008) Trends Cell Biol. , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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., Le M., 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    Le, M.4    Li, J.5    Gygi, S.P.6    Kirschner, M.W.7
  • 22
    • 0035949469 scopus 로고    scopus 로고
    • CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family
    • Ho H.Y., Rohatgi R., Ma L., and Kirschner M.W. CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family. Proc. Natl. Acad. Sci. USA 98 (2001) 11306-11311
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11306-11311
    • Ho, H.Y.1    Rohatgi, R.2    Ma, L.3    Kirschner, M.W.4
  • 23
    • 34250844333 scopus 로고    scopus 로고
    • SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis
    • Yarar D., Waterman-Storer C.M., and Schmid S.L. SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Dev. Cell 13 (2007) 43-56
    • (2007) Dev. Cell , vol.13 , pp. 43-56
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 24
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 25
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel T.P., Boujemaa R., Pantaloni D., and Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401 (1999) 613-616
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 26
    • 55549134613 scopus 로고    scopus 로고
    • EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization
    • Takano K., Toyooka K., and Suetsugu S. EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization. EMBO J. 27 (2008) 2817-2828
    • (2008) EMBO J. , vol.27 , pp. 2817-2828
    • Takano, K.1    Toyooka, K.2    Suetsugu, S.3
  • 27
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R.D., Heuser J.A., and Pollard T.D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95 (1998) 6181-6186
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 28
    • 35848962950 scopus 로고    scopus 로고
    • Amphiphysin 1 is important for actin polymerization during phagocytosis
    • Yamada H., et al. Amphiphysin 1 is important for actin polymerization during phagocytosis. Mol. Biol. Cell 18 (2007) 4669-4680
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4669-4680
    • Yamada, H.1
  • 29
    • 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
  • 30
    • 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


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