메뉴 건너뛰기




Volumn 104, Issue 2, 2013, Pages 396-403

Autoinhibition of endophilin in solution via interdomain interactions

Author keywords

[No Author keywords available]

Indexed keywords

2 ACYLGLYCEROPHOSPHATE ACYLTRANSFERASE; 2-ACYLGLYCEROPHOSPHATE ACYLTRANSFERASE; ACYLTRANSFERASE;

EID: 84872779821     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.12.009     Document Type: Article
Times cited : (24)

References (30)
  • 1
    • 0033539120 scopus 로고    scopus 로고
    • Endophilin i mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid
    • A. Schmidt, and M. Wolde H.D. Söling Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid Nature 401 1999 133 141
    • (1999) Nature , vol.401 , pp. 133-141
    • Schmidt, A.1    Wolde, M.2    Söling, H.D.3
  • 2
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • K. Farsad, and N. Ringstad P. De Camilli 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    De Camilli, P.3
  • 3
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • H.T. McMahon, and J.L. Gallop 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
  • 4
    • 77958496919 scopus 로고    scopus 로고
    • Endophilin functions as a membrane-bending molecule and is delivered to endocytic zones by exocytosis
    • J. Bai, and Z. Hu J.M. Kaplan Endophilin functions as a membrane-bending molecule and is delivered to endocytic zones by exocytosis Cell 143 2010 430 441
    • (2010) Cell , vol.143 , pp. 430-441
    • Bai, J.1    Hu, Z.2    Kaplan, J.M.3
  • 5
    • 70350783743 scopus 로고    scopus 로고
    • Amphipathic motifs in BAR domains are essential for membrane curvature sensing
    • V.K. Bhatia, and K.L. Madsen D. Stamou Amphipathic motifs in BAR domains are essential for membrane curvature sensing EMBO J. 28 2009 3303 3314
    • (2009) EMBO J. , vol.28 , pp. 3303-3314
    • Bhatia, V.K.1    Madsen, K.L.2    Stamou, D.3
  • 6
    • 33745523031 scopus 로고    scopus 로고
    • Mechanism of endophilin N-BAR domain-mediated membrane curvature
    • J.L. Gallop, and C.C. Jao H.T. McMahon Mechanism of endophilin N-BAR domain-mediated membrane curvature EMBO J. 25 2006 2898 2910
    • (2006) EMBO J. , vol.25 , pp. 2898-2910
    • Gallop, J.L.1    Jao, C.C.2    McMahon, H.T.3
  • 7
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • M. Masuda, and S. Takeda N. Mochizuki 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    Mochizuki, N.3
  • 8
    • 79953862815 scopus 로고    scopus 로고
    • Mechanism of membrane curvature sensing by amphipathic helix containing proteins
    • H. Cui, E. Lyman, and G.A. Voth Mechanism of membrane curvature sensing by amphipathic helix containing proteins Biophys. J. 100 2011 1271 1279
    • (2011) Biophys. J. , vol.100 , pp. 1271-1279
    • Cui, H.1    Lyman, E.2    Voth, G.A.3
  • 9
    • 84859175189 scopus 로고    scopus 로고
    • Structural basis of membrane bending by the N-BAR protein endophilin
    • C. Mim, and H. Cui V.M. Unger Structural basis of membrane bending by the N-BAR protein endophilin Cell 149 2012 137 145
    • (2012) Cell , vol.149 , pp. 137-145
    • Mim, C.1    Cui, H.2    Unger, V.M.3
  • 10
    • 72149095496 scopus 로고    scopus 로고
    • SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination
    • J.-F. Trempe, and C.X.-Q. Chen E.A. Fon SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination Mol. Cell 36 2009 1034 1047
    • (2009) Mol. Cell , vol.36 , pp. 1034-1047
    • Trempe, J.-F.1    Chen, C.X.-Q.2    Fon, E.A.3
  • 11
    • 0033199465 scopus 로고    scopus 로고
    • Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis
    • N. Ringstad, and H. Gad P. De Camilli Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis Neuron 24 1999 143 154
    • (1999) Neuron , vol.24 , pp. 143-154
    • Ringstad, N.1    Gad, H.2    De Camilli, P.3
  • 12
    • 81355153885 scopus 로고    scopus 로고
    • Recruitment of endophilin to clathrin-coated pit necks is required for efficient vesicle uncoating after fission
    • I. Milosevic, and S. Giovedi P. De Camilli Recruitment of endophilin to clathrin-coated pit necks is required for efficient vesicle uncoating after fission Neuron 72 2011 587 601
    • (2011) Neuron , vol.72 , pp. 587-601
    • Milosevic, I.1    Giovedi, S.2    De Camilli, P.3
  • 13
    • 53049089051 scopus 로고    scopus 로고
    • Structure and plasticity of endophilin and sorting nexin 9
    • Q. Wang, H.Y.K. Kaan, R.N. Hooda, S.L. Goh, and H. Sondermann Structure and plasticity of endophilin and sorting nexin 9 Structure 16 2008 1574 1587
    • (2008) Structure , vol.16 , pp. 1574-1587
    • Wang, Q.1    Kaan, H.Y.K.2    Hooda, R.N.3    Goh, S.L.4    Sondermann, H.5
  • 14
    • 77952378553 scopus 로고    scopus 로고
    • Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation
    • Y. Rao, and Q. Ma V. Haucke Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation Proc. Natl. Acad. Sci. USA 107 2010 8213 8218
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8213-8218
    • Rao, Y.1    Ma, Q.2    Haucke, V.3
  • 15
    • 84856718085 scopus 로고    scopus 로고
    • Single point mutation in Bin/Amphiphysin/Rvs (BAR) sequence of endophilin impairs dimerization, membrane shaping, and Src homology 3 domain-mediated partnership
    • A. Gortat, and M.J. San-Roman A.A. Schmidt Single point mutation in Bin/Amphiphysin/Rvs (BAR) sequence of endophilin impairs dimerization, membrane shaping, and Src homology 3 domain-mediated partnership J. Biol. Chem. 287 2012 4232 4247
    • (2012) J. Biol. Chem. , vol.287 , pp. 4232-4247
    • Gortat, A.1    San-Roman, M.J.2    Schmidt, A.A.3
  • 16
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • B.J. Mayer SH3 domains: complexity in moderation J. Cell Sci. 114 2001 1253 1263
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 17
    • 38349091489 scopus 로고    scopus 로고
    • Well-tempered metadynamics: A smoothly converging and tunable free-energy method
    • A. Barducci, G. Bussi, and M. Parrinello Well-tempered metadynamics: a smoothly converging and tunable free-energy method Phys. Rev. Lett. 100 2008 020603
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 020603
    • Barducci, A.1    Bussi, G.2    Parrinello, M.3
  • 19
    • 33644769684 scopus 로고    scopus 로고
    • Efficient reconstruction of complex free energy landscapes by multiple walkers metadynamics
    • P. Raiteri, and A. Laio M. Parrinello Efficient reconstruction of complex free energy landscapes by multiple walkers metadynamics J. Phys. Chem. B 110 2006 3533 3539
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3533-3539
    • Raiteri, P.1    Laio, A.2    Parrinello, M.3
  • 20
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • A.D. MacKerell, and D. Bashford M. Karplus All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1    Bashford, D.2    Karplus, M.3
  • 21
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • A.D. Mackerell Jr., M. Feig, and C.L. Brooks 3rd Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25 2004 1400 1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 23
    • 84872826383 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 25
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 26
    • 5544254964 scopus 로고
    • Molecular dynamics simulation for polymers in the presence of a heat bath
    • G.S. Grest, and K. Kremer Molecular dynamics simulation for polymers in the presence of a heat bath Phys. Rev. A 33 1986 3628 3631
    • (1986) Phys. Rev. A , vol.33 , pp. 3628-3631
    • Grest, G.S.1    Kremer, K.2
  • 27
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, and Y. Zhang B.R. Brooks Constant pressure molecular dynamics simulation: the Langevin piston method J. Chem. Phys. 103 1995 4613 4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Brooks, B.R.3
  • 30
    • 69349100797 scopus 로고    scopus 로고
    • PLUMED: A portable plugin for free-energy calculations with molecular dynamics
    • M. Bonomi, and D. Branduardi M. Parrinello PLUMED: a portable plugin for free-energy calculations with molecular dynamics Comput. Phys. Commun. 180 2009 1961 1972
    • (2009) Comput. Phys. Commun. , vol.180 , pp. 1961-1972
    • Bonomi, M.1    Branduardi, D.2    Parrinello, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.