메뉴 건너뛰기




Volumn 584, Issue 6, 2010, Pages 1111-1118

Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II

Author keywords

EFC domain; F BAR domain; Invagination; Membrane; Protrusion

Indexed keywords

AMINO ACID; LIPOSOME; PACSIN 2; PROTEIN; SYNDAPIN II; UNCLASSIFIED DRUG;

EID: 77950368868     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.02.058     Document Type: Article
Times cited : (67)

References (30)
  • 1
    • 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., De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 2006, 1761:897-912.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 2
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
    • Takenawa T., Suetsugu S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2007, 8:37-48.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 4
    • 77950594242 scopus 로고    scopus 로고
    • Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Semin. Cell Dev. Biol. Epub 10.1016/j.semcdb.2009.12.002.
    • Suetsugu, S., Toyooka, K. and Senju, Y. (2009). Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Semin. Cell Dev. Biol. Epub 10.1016/j.semcdb.2009.12.002.
    • (2009)
    • Suetsugu, S.1    Toyooka, K.2    Senju, Y.3
  • 7
    • 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., Mochizuki N. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 2006, 25:2889-2897.
    • (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
  • 8
    • 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. Dev. Cell 2005, 9:791-804.
    • (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
  • 9
    • 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., 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. 2006, 172:269-279.
    • (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
  • 10
    • 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 2007, 129:761-772.
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1
  • 11
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature
    • Henne W.M., et al. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 2007, 15:839-852.
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1
  • 12
    • 77449095272 scopus 로고    scopus 로고
    • The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration
    • Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T. The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration. Sci. Signal. 2009, 2:ra52.
    • (2009) Sci. Signal. , vol.2
    • Itoh, T.1    Hasegawa, J.2    Tsujita, K.3    Kanaho, Y.4    Takenawa, T.5
  • 13
    • 69449100707 scopus 로고    scopus 로고
    • The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis
    • Guerrier S., et al. The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis. Cell 2009, 138:990-1004.
    • (2009) Cell , vol.138 , pp. 990-1004
    • Guerrier, S.1
  • 14
    • 0030770817 scopus 로고    scopus 로고
    • FAP52, a novel, SH3 domain-containing focal adhesion protein
    • Merilainen J., Lehto V.P., Wasenius V.M. FAP52, a novel, SH3 domain-containing focal adhesion protein. J. Biol. Chem. 1997, 272:23278-23284.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23278-23284
    • Merilainen, J.1    Lehto, V.P.2    Wasenius, V.M.3
  • 15
    • 0033016181 scopus 로고    scopus 로고
    • PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins
    • Ritter B., Modregger J., Paulsson M., Plomann M. PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins. FEBS Lett. 1999, 454:356-362.
    • (1999) FEBS Lett. , vol.454 , pp. 356-362
    • Ritter, B.1    Modregger, J.2    Paulsson, M.3    Plomann, M.4
  • 16
    • 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., Kelly R.B. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 1999, 10:501-513.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 17
    • 77949513739 scopus 로고    scopus 로고
    • Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development
    • Edeling M.A., et al. Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development. PLoS One 2009, 4:e8150.
    • (2009) PLoS One , vol.4
    • Edeling, M.A.1
  • 18
    • 70350348378 scopus 로고    scopus 로고
    • F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis
    • Dharmalingam E., Haeckel A., Pinyol R., Schwintzer L., Koch D., Kessels M.M., Qualmann B. F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis. J. Neurosci. 2009, 29:13315-13327.
    • (2009) J. Neurosci. , vol.29 , pp. 13315-13327
    • Dharmalingam, E.1    Haeckel, A.2    Pinyol, R.3    Schwintzer, L.4    Koch, D.5    Kessels, M.M.6    Qualmann, B.7
  • 20
    • 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. 2006, 281:35347-35358.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35347-35358
    • Suetsugu, S.1
  • 21
    • 85011045864 scopus 로고
    • Quantification of polyphosphoinositides using selected ion monitoring electrospray mass spectrometry
    • Michelsen P., Jergil B., Odham G. Quantification of polyphosphoinositides using selected ion monitoring electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 1995, 9:1109-1114.
    • (1995) Rapid Commun. Mass Spectrom. , vol.9 , pp. 1109-1114
    • Michelsen, P.1    Jergil, B.2    Odham, G.3
  • 22
    • 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., Suetsugu S. EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization. EMBO J. 2008, 27:2817-2828.
    • (2008) EMBO J. , vol.27 , pp. 2817-2828
    • Takano, K.1    Toyooka, K.2    Suetsugu, S.3
  • 23
    • 70350307197 scopus 로고    scopus 로고
    • The direction of actin polymerization for vesicle fission suggested from membranes tubulated by the EFC/F-BAR domain protein FBP17
    • Suetsugu S. The direction of actin polymerization for vesicle fission suggested from membranes tubulated by the EFC/F-BAR domain protein FBP17. FEBS Lett. 2009, 583:3401-3404.
    • (2009) FEBS Lett. , vol.583 , pp. 3401-3404
    • Suetsugu, S.1
  • 24
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T., Ibata K., Park E.S., Kubota M., Mikoshiba K., Miyawaki A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: a new software suite for macromolecular structure determination
    • Brunger A.T., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D 1998, 54(Pt 5):905-921.
    • (1998) Acta Crystallogr., Sect. D , vol.54 , Issue.PART 5 , pp. 905-921
    • Brunger, A.T.1
  • 29
    • 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., Suetsugu S. IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol. 2008, 18:52-60.
    • (2008) Trends Cell Biol. , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.