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Volumn 320, Issue 3, 2004, Pages 1034-1042

RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes

Author keywords

BAR domain; ER; Membrane deformation; Rho; RhoGAP

Indexed keywords

AMPHIPHYSIN; CROSS LINKING REAGENT; ENDOPHILIN A1; ENDOPHILIN A2; ENDOPHILIN A3; ENDOPHILIN B1; ENDOPHILIN B2; LIPOSOME; MEMBRANE LIPID; OLIGOMER; PROTEIN; RHO FACTOR; RHOGAP INTERACTING WITH CIP4 HOMOLOGS 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 3042717086     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.221     Document Type: Article
Times cited : (42)

References (24)
  • 2
    • 0035446006 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis: Membrane factors pull the trigger
    • Takei K., Haucke V. Clathrin-mediated endocytosis: membrane factors pull the trigger. Trends Cell Biol. 11:2001;385-391
    • (2001) Trends Cell Biol. , vol.11 , pp. 385-391
    • Takei, K.1    Haucke, V.2
  • 3
    • 0342748583 scopus 로고    scopus 로고
    • Sequential steps in clathrin-mediated synaptic vesicle endocytosis
    • Brodin L., Low P., Shupliakov O. Sequential steps in clathrin-mediated synaptic vesicle endocytosis. Curr. Opin. Neurobiol. 10:2000;312-320
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 312-320
    • Brodin, L.1    Low, P.2    Shupliakov, O.3
  • 4
    • 0032503947 scopus 로고    scopus 로고
    • Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes
    • Takei K., Haucke V., Slepnev V., Farsad K., Salazar M., Chen H., De Camilli P. Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell. 94:1998;131-141
    • (1998) Cell , vol.94 , pp. 131-141
    • Takei, K.1    Haucke, V.2    Slepnev, V.3    Farsad, K.4    Salazar, M.5    Chen, H.6    De Camilli, P.7
  • 5
    • 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. 93:1998;1021-1029
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 6
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., 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
  • 7
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol. 155:2001;193-200
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 9
    • 0037131521 scopus 로고    scopus 로고
    • Endocytosis: Driving membranes around the bend
    • Hurley J.H., Wendland B. Endocytosis: driving membranes around the bend. Cell. 111:2002;143-146
    • (2002) Cell , vol.111 , pp. 143-146
    • Hurley, J.H.1    Wendland, B.2
  • 10
    • 1842483252 scopus 로고    scopus 로고
    • Membrane curvature: How BAR domains bend bilayers
    • Zimmerberg J., McLaughlin S. Membrane curvature: how BAR domains bend bilayers. Curr. Biol. 14:2004;R250-252
    • (2004) Curr. Biol. , vol.14 , pp. 250-252
    • Zimmerberg, J.1    McLaughlin, S.2
  • 11
    • 1342331452 scopus 로고    scopus 로고
    • Cell biology. BAR domains go on a bender
    • Lee M.C., Schekman R. Cell biology. BAR domains go on a bender. Science. 303:2004;479-480
    • (2004) Science , vol.303 , pp. 479-480
    • Lee, M.C.1    Schekman, R.2
  • 13
    • 0029741917 scopus 로고    scopus 로고
    • BIN1 is a novel MYC-interacting protein with features of a tumour suppressor
    • Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C. BIN1 is a novel MYC-interacting protein with features of a tumour suppressor. Nat. Genet. 14:1996;69-77
    • (1996) Nat. Genet. , vol.14 , pp. 69-77
    • Sakamuro, D.1    Elliott, K.J.2    Wechsler-Reya, R.3    Prendergast, G.C.4
  • 15
    • 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
  • 16
    • 0035860812 scopus 로고    scopus 로고
    • Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1
    • Richnau N., Aspenström P. Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J. Biol. Chem. 276:2001;35060-35070
    • (2001) J. Biol. Chem. , vol.276 , pp. 35060-35070
    • Richnau, N.1    Aspenström, P.2
  • 17
    • 0038521292 scopus 로고    scopus 로고
    • TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport
    • Chiang S.H., Hwang J., Legendre M., Zhang M., Kimura A., Saltiel A.R. TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport. EMBO J. 22:2003;2679-2691
    • (2003) EMBO J. , vol.22 , pp. 2679-2691
    • Chiang, S.H.1    Hwang, J.2    Legendre, M.3    Zhang, M.4    Kimura, A.5    Saltiel, A.R.6
  • 18
    • 0037213689 scopus 로고    scopus 로고
    • Rho GTPase-activating proteins in cell regulation
    • Moon S.Y., Zheng Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 13:2003;13-22
    • (2003) Trends Cell Biol. , vol.13 , pp. 13-22
    • Moon, S.Y.1    Zheng, Y.2
  • 19
    • 0037174150 scopus 로고    scopus 로고
    • Human RhoGAP domain-containing proteins: Structure, function and evolutionary relationships
    • Peck J., Douglas G.t., Wu C.H., Burbelo P.D. Human RhoGAP domain-containing proteins: structure, function and evolutionary relationships. FEBS Lett. 528:2002;27-34
    • (2002) FEBS Lett. , vol.528 , pp. 27-34
    • Peck, J.1    T., D.G.2    Wu, C.H.3    Burbelo, P.D.4
  • 21
    • 0036651754 scopus 로고    scopus 로고
    • Amphiphysins: Raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp
    • Zhang B., Zelhof A.C. Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp. Traffic. 3:2002;452-460
    • (2002) Traffic , vol.3 , pp. 452-460
    • Zhang, B.1    Zelhof, A.C.2
  • 22
    • 0033527653 scopus 로고    scopus 로고
    • The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity
    • Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A., Migone N., Hoffmuller U., Schneider-Mergener J., Cesareni G. The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity. J. Biol. Chem. 274:1999;32001-32007
    • (1999) J. Biol. Chem. , vol.274 , pp. 32001-32007
    • Cestra, G.1    Castagnoli, L.2    Dente, L.3    Minenkova, O.4    Petrelli, A.5    Migone, N.6    Hoffmuller, U.7    Schneider-Mergener, J.8    Cesareni, G.9
  • 23
    • 0037423214 scopus 로고    scopus 로고
    • Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1
    • Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M. Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1. J. Biol. Chem. 278:2003;4160-4167
    • (2003) J. Biol. Chem. , vol.278 , pp. 4160-4167
    • Modregger, J.1    Schmidt, A.A.2    Ritter, B.3    Huttner, W.B.4    Plomann, M.5
  • 24
    • 0034711313 scopus 로고    scopus 로고
    • Nadrin, a novel neuron-specific GTPase-activating protein involved in regulated exocytosis
    • Harada A., Furuta B., Takeuchi K., Itakura M., Takahashi M., Umeda M. Nadrin, a novel neuron-specific GTPase-activating protein involved in regulated exocytosis. J. Biol. Chem. 275:2000;36885-36891
    • (2000) J. Biol. Chem. , vol.275 , pp. 36885-36891
    • Harada, A.1    Furuta, B.2    Takeuchi, K.3    Itakura, M.4    Takahashi, M.5    Umeda, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.