메뉴 건너뛰기




Volumn 15, Issue 7, 2007, Pages 839-852

Structure and Analysis of FCHo2 F-BAR Domain: A Dimerizing and Membrane Recruitment Module that Effects Membrane Curvature

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; LIPOSOME; MEMBRANE PROTEIN;

EID: 34447256592     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.05.002     Document Type: Article
Times cited : (242)

References (48)
  • 1
    • 0030855279 scopus 로고    scopus 로고
    • Bias reduction in phase refinement by modified interference functions: introducing the γ function
    • Abrahams J.P. Bias reduction in phase refinement by modified interference functions: introducing the γ function. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 371-376
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 371-376
    • Abrahams, J.P.1
  • 2
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach C., Greenhalgh D.A., Khorana H.G., and Hubbell W.L. A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 91 (1994) 1667-1671
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 3
    • 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
  • 4
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G., Vonrhein C., Flensburg C., Schiltz M., and Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 2023-2030
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 5
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides
    • Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T., and Cullen P.J. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr. Biol. 14 (2004) 1791-1800
    • (2004) Curr. Biol. , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5    Mellor, H.6    Klumperman, J.7    McMahon, H.T.8    Cullen, P.J.9
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for X-ray crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 23844504558 scopus 로고    scopus 로고
    • Human Gas7 isoforms homologous to mouse transcripts differentially induce neurite outgrowth
    • Chao C.C., Chang P.Y., and Lu H.H. Human Gas7 isoforms homologous to mouse transcripts differentially induce neurite outgrowth. J. Neurosci. Res. 81 (2005) 153-162
    • (2005) J. Neurosci. Res. , vol.81 , pp. 153-162
    • Chao, C.C.1    Chang, P.Y.2    Lu, H.H.3
  • 8
    • 33847343505 scopus 로고    scopus 로고
    • Pombe Cdc15 homology (PCH) proteins: coordinators of membrane-cytoskeletal interactions
    • Chitu V., and Stanley E.R. Pombe Cdc15 homology (PCH) proteins: coordinators of membrane-cytoskeletal interactions. Trends Cell Biol. 17 (2007) 145-156
    • (2007) Trends Cell Biol. , vol.17 , pp. 145-156
    • Chitu, V.1    Stanley, E.R.2
  • 9
    • 1342312355 scopus 로고    scopus 로고
    • Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila
    • Coyle I.P., Koh Y.H., Lee W.C., Slind J., Fergestad T., Littleton J.T., and Ganetzky B. Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila. Neuron 41 (2004) 521-534
    • (2004) Neuron , vol.41 , pp. 521-534
    • Coyle, I.P.1    Koh, Y.H.2    Lee, W.C.3    Slind, J.4    Fergestad, T.5    Littleton, J.T.6    Ganetzky, B.7
  • 10
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276 (1997) 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • de la Fortelle, E.1    Bricogne, G.2
  • 11
    • 33646830138 scopus 로고    scopus 로고
    • A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer
    • Delfino F.J., Stevenson H., and Smithgall T.E. A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer. J. Biol. Chem. 281 (2006) 8829-8835
    • (2006) J. Biol. Chem. , vol.281 , pp. 8829-8835
    • Delfino, F.J.1    Stevenson, H.2    Smithgall, T.E.3
  • 15
    • 0037202289 scopus 로고    scopus 로고
    • Cloning of rat ARHGAP4/C1, a RhoGAP family member expressed in the nervous system that colocalizes with the Golgi complex and microtubules
    • Foletta V.C., Brown F.D., and Young III W.S. Cloning of rat ARHGAP4/C1, a RhoGAP family member expressed in the nervous system that colocalizes with the Golgi complex and microtubules. Brain Res. Mol. Brain Res. 107 (2002) 65-79
    • (2002) Brain Res. Mol. Brain Res. , vol.107 , pp. 65-79
    • Foletta, V.C.1    Brown, F.D.2    Young III, W.S.3
  • 19
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: a case of bending and binding?
    • Habermann B. The BAR-domain family of proteins: a case of bending and binding?. EMBO Rep. 5 (2004) 250-255
    • (2004) EMBO Rep. , vol.5 , pp. 250-255
    • Habermann, B.1
  • 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
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell W.L., Cafiso D.S., and Altenbach C. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7 (2000) 735-739
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G. Distance measurements in the nanometer range by pulse EPR. ChemPhysChem 3 (2002) 927-932
    • (2002) ChemPhysChem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 26
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • Jeschke G., Koch A., Jonas U., and Godt A. Direct conversion of EPR dipolar time evolution data to distance distributions. J. Magn. Reson. 155 (2002) 72-82
    • (2002) J. Magn. Reson. , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 27
    • 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
  • 28
    • 33749405211 scopus 로고    scopus 로고
    • Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination
    • Kakimoto T., Katoh H., and Negishi M. Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination. J. Biol. Chem. 281 (2006) 29042-29053
    • (2006) J. Biol. Chem. , vol.281 , pp. 29042-29053
    • Kakimoto, T.1    Katoh, H.2    Negishi, M.3
  • 29
    • 16644374517 scopus 로고    scopus 로고
    • Identification and characterization of human FCHO2 and mouse Fcho2 genes in silico
    • Katoh M., and Katoh M. Identification and characterization of human FCHO2 and mouse Fcho2 genes in silico. Int. J. Mol. Med. 14 (2004) 327-331
    • (2004) Int. J. Mol. Med. , vol.14 , pp. 327-331
    • Katoh, M.1    Katoh, M.2
  • 30
    • 0029003669 scopus 로고
    • The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors
    • Kim L., and Wong T.W. The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors. Mol. Cell. Biol. 15 (1995) 4553-4561
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4553-4561
    • Kim, L.1    Wong, T.W.2
  • 31
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure
    • Langen R., Oh K.J., Cascio D., and Hubbell W.L. Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry 39 (2000) 8396-8405
    • (2000) Biochemistry , vol.39 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 32
    • 33846817369 scopus 로고    scopus 로고
    • Structural basis for the actin-binding function of missing-in-metastasis
    • Lee S.H., Kerff F., Chereau D., Ferron F., Klug A., and Dominguez R. Structural basis for the actin-binding function of missing-in-metastasis. Structure 15 (2007) 145-155
    • (2007) Structure , vol.15 , pp. 145-155
    • Lee, S.H.1    Kerff, F.2    Chereau, D.3    Ferron, F.4    Klug, A.5    Dominguez, R.6
  • 33
  • 34
    • 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
  • 35
    • 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
  • 37
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms 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
  • 38
  • 40
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M., Veit S., Godt A., Jeschke G., and Spiess H.W. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142 (2000) 331-340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 43
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann B., Roos J., DiGregorio P.J., and Kelly R.B. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 10 (1999) 501-513
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 44
    • 33748295539 scopus 로고    scopus 로고
    • Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN
    • Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R., Muller-Esterl W., and Icking A. Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN. Mol. Biol. Cell 17 (2006) 3870-3880
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3870-3880
    • Schilling, K.1    Opitz, N.2    Wiesenthal, A.3    Oess, S.4    Tikkanen, R.5    Muller-Esterl, W.6    Icking, A.7
  • 45
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways
    • Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J., and Smerdon S.J. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 411 (2001) 215-219
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3    Walker, P.A.4    Rittinger, K.5    Gamblin, S.J.6    Smerdon, S.J.7
  • 46
    • 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
  • 47
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Uson I., and Sheldrick G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9 (1999) 643-648
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 48
    • 22544482948 scopus 로고    scopus 로고
    • Crystal structure of the endophilin-A1 BAR domain
    • Weissenhorn W. Crystal structure of the endophilin-A1 BAR domain. J. Mol. Biol. 351 (2005) 653-661
    • (2005) J. Mol. Biol. , vol.351 , pp. 653-661
    • Weissenhorn, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.