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Volumn 97, Issue 10, 2009, Pages 2727-2735

Membrane-bending mechanism of amphiphysin N-BAR domains

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPHYSIN; MOLECULAR SCAFFOLD;

EID: 72049092011     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.08.051     Document Type: Article
Times cited : (98)

References (42)
  • 1
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh, M., and H. T. McMahon. 1999. The structural era of endocytosis. Science. 285:215-220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 3
    • 0041765833 scopus 로고    scopus 로고
    • Mechanisms of membrane deformation
    • Farsad, K., and P. D. Camilli. 2003. Mechanisms of membrane deformation. Curr. Opin. Cell Biol. 15:372-381.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 372-381
    • Farsad, K.1    Camilli, P.D.2
  • 4
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • McMahon, H. T., and I. G. Hills. 2004. COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr. Opin. Cell Biol. 16:379-391.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 379-391
    • McMahon, H.T.1    Hills, I.G.2
  • 5
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • DOI 10.1038/nature04396
    • McMahon, H. T., and J. L. Gallop. 2005. Membrane curvature and mechanisms of dynamic cell membrane remodeling. Nature. 438:590-596. (Pubitemid 41740562)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 6
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho, W., and R. V. Stahelin. 2005. Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 296:153-161.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.296 , pp. 153-161
    • Cho, W.1    Stahelin, R.V.2
  • 8
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. 2008. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9:99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 9
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei, K., V. I. Slepnev, V. Haucke, and P. De Camilli. 1999. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat. Cell Biol. 1:33-39.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 10
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • Peter, B. J., H. M. Kent, I. G. Mills, Y. Vallis, P. J. G. Butler, et al. 2004. BAR domains as sensors of membrane curvature: The amphiphysin BAR structure. Science. 303:495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5
  • 12
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring, S., and J. Sturgis. 2005. Chromatic adaptation of photosynthetic membranes. Science. 309:484-487.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.2
  • 13
    • 33748578027 scopus 로고    scopus 로고
    • AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes
    • Scheuring, S. 2006. AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes. Curr. Opin. Struct. Biol. 10:1-7.
    • (2006) Curr. Opin. Struct. Biol. , vol.10 , pp. 1-7
    • Scheuring, S.1
  • 15
    • 50649105102 scopus 로고    scopus 로고
    • Toward a biomechanical understanding of whole bacterial cells
    • Morris, D. M., and G. J. Jensen. 2008. Toward a biomechanical understanding of whole bacterial cells. Annu. Rev. Biochem. 77:583-613.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 583-613
    • Morris, D.M.1    Jensen, G.J.2
  • 16
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg, J., and M. M. Kozlov. 2006. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7:9-19.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 17
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo, F., H. T. McMahon, and M. M. Kozlov. 2008. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys. J. 95:2325-2339.
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 18
    • 33750037303 scopus 로고    scopus 로고
    • Direct observation of Bin/amphiphysin/ Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations
    • Blood, P. D., and G. A. Voth. 2006. Direct observation of Bin/amphiphysin/ Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations. Proc. Natl. Acad. Sci. USA. 103:15068-15072.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15068-15072
    • Blood, P.D.1    Voth, G.A.2
  • 19
    • 53249125167 scopus 로고    scopus 로고
    • Four-scale description of membrane sculpting by BAR domains
    • Arkhipov, A., Y. Yin, and K. Schulten. 2008. Four-scale description of membrane sculpting by BAR domains. Biophys. J. 95:2806-2821.
    • (2008) Biophys. J. , vol.95 , pp. 2806-2821
    • Arkhipov, A.1    Yin, Y.2    Schulten, K.3
  • 20
    • 55549109763 scopus 로고    scopus 로고
    • Intrinsic curvature properties of photosynthetic proteins in chromatophores
    • Chandler, D., J. Hsin, C. B. Harrison, J. Gumbart, and K. Schulten. 2008. Intrinsic curvature properties of photosynthetic proteins in chromatophores. Biophys. J. 95:2822-2836.
    • (2008) Biophys. J. , vol.95 , pp. 2822-2836
    • Chandler, D.1    Hsin, J.2    Harrison, C.B.3    Gumbart, J.4    Schulten, K.5
  • 21
    • 66349103875 scopus 로고    scopus 로고
    • Simulations of membrane tubulation by lattices of amphiphysin N-BAR domains
    • Yin, Y., A. Arkhipov, and K. Schulten. 2009. Simulations of membrane tubulation by lattices of amphiphysin N-BAR domains. Structure. 17:882-892.
    • (2009) Structure , vol.17 , pp. 882-892
    • Yin, Y.1    Arkhipov, A.2    Schulten, K.3
  • 22
  • 23
    • 50349086997 scopus 로고    scopus 로고
    • Factors influencing local membrane curvature induction by N-BAR domains as revealed by molecular dynamics simulations
    • Blood, P. D., R. D. Swenson, and G. A. Voth. 2008. Factors influencing local membrane curvature induction by N-BAR domains as revealed by molecular dynamics simulations. Biophys. J. 95:1866-1876.
    • (2008) Biophys. J. , vol.95 , pp. 1866-1876
    • Blood, P.D.1    Swenson, R.D.2    Voth, G.A.3
  • 25
    • 58149164579 scopus 로고    scopus 로고
    • Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers
    • Löw, C., U. Weininger, H. Lee, K. Schweimer, I. Neundorf, et al. 2008. Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. Biophys. J. 95:4315-4323.
    • (2008) Biophys. J. , vol.95 , pp. 4315-4323
    • Löw, C.1    Weininger, U.2    Lee, H.3    Schweimer, K.4    Neundorf, I.5
  • 26
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • DOI 10.1021/bi962252b
    • Antonny, B., S. Beraud-Dufour, P. Chardin, and M. Chabre. 1997. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry. 36:4675-4684. (Pubitemid 27180318)
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 28
  • 29
    • 33845204189 scopus 로고    scopus 로고
    • Stability and Dynamics of Virus Capsids Described by Coarse-Grained Modeling
    • DOI 10.1016/j.str.2006.10.003, PII S0969212606004023
    • Arkhipov, A., P. L. Freddolino, and K. Schulten. 2006. Stability and dynamics of virus capsids described by coarse-grained modeling. Structure. 14:1767-1777. (Pubitemid 44855625)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1767-1777
    • Arkhipov, A.1    Freddolino, P.L.2    Schulten, K.3
  • 30
    • 84873517979 scopus 로고    scopus 로고
    • Multi-scale simulations of membrane sculpting by N-BAR domains
    • P. Biggin and M. Sansom, editors. Royal Society of Chemistry, London, UK
    • Yin, Y., A. Arkhipov, and K. Schulten. 2009. Multi-scale simulations of membrane sculpting by N-BAR domains. In Molecular Simulations and Biomembranes: From Biophysics to Function. P. Biggin and M. Sansom, editors. Royal Society of Chemistry, London, UK.
    • (2009) Molecular Simulations and Biomembranes: From Biophysics to Function
    • Yin, Y.1    Arkhipov, A.2    Schulten, K.3
  • 34
    • 33745523031 scopus 로고    scopus 로고
    • Mechanism of endophilin N-BAR domain-mediated membrane curvature
    • Gallop, J. L., C. C. Jao, H. M. Kent, P. J. Butler, P. R. Evans, et al. 2006. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J. 25:2898-2910.
    • (2006) EMBO J. , vol.25 , pp. 2898-2910
    • Gallop, J.L.1    Jao, C.C.2    Kent, H.M.3    Butler, P.J.4    Evans, P.R.5
  • 35
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • Isralewitz, B., M. Gao, and K. Schulten. 2001. Steered molecular dynamics and mechanical functions of proteins. Curr. Opin. Struct. Biol. 11:224-230.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 36
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor, M., and K. Schulten. 2007. Single-molecule experiments in vitro and in silico. Science. 316:1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 38
    • 0033758069 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid bilayers
    • Feller, S. E. 2000. Molecular dynamics simulations of lipid bilayers. Curr. Opin. Colloid Interface Sci. 5:217-223.
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 217-223
    • Feller, S.E.1
  • 41
    • 22544482948 scopus 로고    scopus 로고
    • Crystal structure of the endophilin-A1 BAR domain
    • Weissenhorn, W. 2005. Crystal structure of the endophilin-A1 BAR domain. J. Mol. Biol. 351:653-661.
    • (2005) J. Mol. Biol. , vol.351 , pp. 653-661
    • Weissenhorn, W.1
  • 42
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • DOI 10.1038/sj.emboj.7601176, PII 7601176
    • Masuda, M., S. Takeda, M. Sone, T. Ohki, H. Mori, et al. 2006. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 25:2889-2897. (Pubitemid 43980395)
    • (2006) EMBO Journal , vol.25 , Issue.12 , pp. 2889-2897
    • Masuda, M.1    Takeda, S.2    Sone, M.3    Ohki, T.4    Mori, H.5    Kamioka, Y.6    Mochizuki, N.7


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