메뉴 건너뛰기




Volumn 11, Issue 4, 2011, Pages 272-282

Attachment of rod-like (BAR) proteins and membrane shape

Author keywords

AFM; Attachment dynamics; Curvature membrane proteins; Membrane shape

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; PROTEIN BAR; UNCLASSIFIED DRUG;

EID: 79954517705     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/138955711795305353     Document Type: Article
Times cited : (38)

References (58)
  • 1
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad, K.; Ringstad, N.; Takei, K.; Floyd, S.; Rose, K.; Camilli, P.D. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol., 2001, 155, 193-200.
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.4    Rose, K.5    Camilli, P.D.6
  • 2
    • 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.; Rittinger, K.; Gamblin, S.; Smerdon, S. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature, 2001, 411, 215-219.
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3    Walker, P.4    Rittinger, K.5    Gamblin, S.6    Smerdon, S.7
  • 3
    • 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.; Camilli, P.D. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell, 2005, 23, 791-804.
    • (2005) Dev. Cell , vol.23 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    Camilli, P.D.6
  • 5
    • 36849073141 scopus 로고    scopus 로고
    • Phase transitions of the coupled membranecytoskeleton modify cellular shape
    • Veksler, A.; Gov, N.S. Phase transitions of the coupled membranecytoskeleton modify cellular shape. Biophys. J., 2007, 93, 3798-3810.
    • (2007) Biophys. J. , vol.93 , pp. 3798-3810
    • Veksler, A.1    Gov, N.S.2
  • 6
    • 64249110493 scopus 로고    scopus 로고
    • The BAR Domain Superfamily: Membrane-Molding Macromolecules
    • Frost, A.; Unger, V.; Camilli, P.D. The BAR Domain Superfamily: Membrane-Molding Macromolecules. Cell, 2009, 137, 191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.2    Camilli, P.D.3
  • 9
    • 29044445245 scopus 로고    scopus 로고
    • Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell cell adhesion: Expression and function in renal cell carcinoma
    • Tsujia, E.; Tsujia, Y.; Fujiwarac, T.;Ogatad, S.; Tsukamotob, K.; Sakub, K. Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell cell adhesion: expression and function in renal cell carcinoma. Biochem. Biophys. Res. Commun. 2006, 339, 1083-1088.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 1083-1088
    • Tsujia, E.1    Tsujia, Y.2    Fujiwarac, T.3    Ogatad, S.4    Tsukamotob, K.5    Sakub, K.6
  • 10
    • 0036796261 scopus 로고    scopus 로고
    • PACSIN1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains
    • Modregger, J.; DiProspero, N.; Charles, V.; Tagle, D.; Plomann, M. PACSIN1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum. Mol. Genet. 2002, 11, 2547-2558.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.2    Charles, V.3    Tagle, D.4    Plomann, M.5
  • 11
    • 0344838402 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 binds to huntingtin: Neuropathologic and biological evidence for a role in Huntington's disease
    • Holbert, S.; Dedeoglu, A.; Humbert, S.; Saudou, F.; Ferrante, R.; Neri, C. Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease. Proc. Natl. Acad. Sci. USA, 2003, 100, 2712-2717.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2712-2717
    • Holbert, S.1    Dedeoglu, A.2    Humbert, S.3    Saudou, F.4    Ferrante, R.5    Neri, C.6
  • 14
    • 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 in Cell Biol., 2008, 18, 52-60.
    • (2008) Trends in Cell Biol. , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4
  • 16
    • 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.; Camilli, P.D. 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    Camilli, P.D.2
  • 17
    • 47649101649 scopus 로고    scopus 로고
    • F-BAR domains: Multifunctional regulators of membrane curvature
    • Heath, R. J.W.; Insall, R.H. F-BAR domains: multifunctional regulators of membrane curvature. J. Cell Sci. 2008, 121, 1951-1954.
    • (2008) J. Cell Sci. , vol.121 , pp. 1951-1954
    • Heath, R.J.W.1    Insall, R.H.2
  • 19
    • 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., 2004, 14, 250-252.
    • (2004) Curr. Biol. , vol.14 , pp. 250-252
    • Zimmerberg, J.1    McLaughlin, S.2
  • 20
    • 34447503425 scopus 로고    scopus 로고
    • Elastic properties of biological membranes influenced by attached proteins
    • Iglič, A.; Slivnik, T.; Kralj-Iglič, V. Elastic properties of biological membranes influenced by attached proteins. J. Biomech., 2007, 40, 2492-2500.
    • (2007) J. Biomech. , vol.40 , pp. 2492-2500
    • Iglič, A.1    Slivnik, T.2    Kralj-Iglič, V.3
  • 21
    • 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.; Niwa, H.; Tsujita, K.; Suetsugu, S.; Nitta, K.; 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    Niwa, H.2    Tsujita, K.3    Suetsugu, S.4    Nitta, K.5
  • 22
    • 0018033380 scopus 로고
    • The structure and function of the myocardial cell surface
    • Langer, G.A. The structure and function of the myocardial cell surface. AJP-Heart and Circ. Phys., 1978, 235, 461-468.
    • (1978) AJP-Heart and Circ. Phys. , vol.235 , pp. 461-468
    • Langer, G.A.1
  • 24
    • 0024378918 scopus 로고
    • Hydration Forces Between Phospholipid Bilayers
    • Rand, R.; Parsegian, V. Hydration Forces Between Phospholipid Bilayers. Biochim. Biophys. Acta, 1989, 988, 351.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351
    • Rand, R.1    Parsegian, V.2
  • 25
    • 0035423783 scopus 로고    scopus 로고
    • Force as a probe of membrane protein structure and function
    • Leckband, D. Force as a probe of membrane protein structure and function. Curr. Opin. Colloid Interface Sci., 2001, 11, 433-439.
    • (2001) Curr. Opin. Colloid Interface Sci. , vol.11 , pp. 433-439
    • Leckband, D.1
  • 27
    • 0027284002 scopus 로고
    • Hydration and steric pressures between phospholipid bilayers
    • McIntosh, T.; Simon, S. Hydration and steric pressures between phospholipid bilayers. Biochemistry, 1993, 32, 8374.
    • (1993) Biochemistry , vol.32 , pp. 8374
    • McIntosh, T.1    Simon, S.2
  • 28
    • 77955269400 scopus 로고    scopus 로고
    • Excluded volume effect and orientation ordering near charged surface in solution of ions and langevin dipoles
    • Iglič, A.; Gongadze, E.; Bohinc, K. Excluded volume effect and orientation ordering near charged surface in solution of ions and langevin dipoles. Bioelectrochemistry, 2010, 79, 223-227.
    • (2010) Bioelectrochemistry , vol.79 , pp. 223-227
    • Iglič, A.1    Gongadze, E.2    Bohinc, K.3
  • 29
    • 0034173153 scopus 로고    scopus 로고
    • Adhesive switching of membranes: Experiment and theory
    • Bruinsma, R.; Behrisch, A.; Sackmann, E. Adhesive switching of membranes: experiment and theory. Phys. Rev. E, 2000, 61, 4253.
    • (2000) Phys. Rev. E , vol.61 , pp. 4253
    • Bruinsma, R.1    Behrisch, A.2    Sackmann, E.3
  • 30
    • 33750037303 scopus 로고    scopus 로고
    • Direct observation of bin/amphiphysin/rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations
    • Blood, P.; Voth, G. Direct observation of bin/amphiphysin/rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations. PNAS, 2006, 103, 15068-15072.
    • (2006) PNAS , vol.103 , pp. 15068-15072
    • Blood, P.1    Voth, G.2
  • 31
    • 0033031748 scopus 로고    scopus 로고
    • Binding of peripheral proteins to mixed lipid membranes: Effect of lipid demixing upon binding
    • Heimburg, T.; Angerstein, B.; Marsh, D. Binding of peripheral proteins to mixed lipid membranes: effect of lipid demixing upon binding. Biophys. J., 1999, 76, 2575-2586.
    • (1999) Biophys. J. , vol.76 , pp. 2575-2586
    • Heimburg, T.1    Angerstein, B.2    Marsh, D.3
  • 32
    • 70349301623 scopus 로고    scopus 로고
    • Monte Carlo simulations of complex formation between a mixed fluid vesicle and a charged colloid
    • Fošnarič, A.; Iglič, A., Kroll, D.; May, S. Monte Carlo simulations of complex formation between a mixed fluid vesicle and a charged colloid. J. Chem. Phys., 2009, 131, 105103.
    • (2009) J. Chem. Phys. , vol.131 , pp. 105103
    • Fošnarič, A.1    Iglič, A.2    Kroll, D.3    May, S.4
  • 33
    • 70350011898 scopus 로고    scopus 로고
    • Modeling membrane deformations and lipid demixing upon protein-membrane interaction: The BAR dimer adsorption
    • Khelashvili, G.; Harries, D.; Weinstein, H. Modeling membrane deformations and lipid demixing upon protein-membrane interaction: The BAR dimer adsorption. Biophys. J., 2009, 97, 1626-1635.
    • (2009) Biophys. J. , vol.97 , pp. 1626-1635
    • Khelashvili, G.1    Harries, D.2    Weinstein, H.3
  • 36
    • 0035102331 scopus 로고    scopus 로고
    • Energetics of clathrin basket assembly
    • Nossal, R. Energetics of clathrin basket assembly. Traffic, 2001, 2, 138-147.
    • (2001) Traffic , vol.2 , pp. 138-147
    • Nossal, R.1
  • 37
    • 0004097995 scopus 로고    scopus 로고
    • Theory of Elasticity
    • Butterworth-Heinemann, Oxford, Vol. 2nd ed
    • Landau, L.; Lifshitz, E. Theory of Elasticity; Butterworth-Heinemann, Oxford, 1996; Vol. 2nd ed., pp 67-70.
    • (1996) , pp. 67-70
    • Landau, L.1    Lifshitz, E.2
  • 38
    • 77952584795 scopus 로고    scopus 로고
    • Mechanical stability of membrane nanotubular protrusions influenced by attachment of flexible rod-like protein
    • Perutková, S.; Kralj-Iglič, V.; Frank, M.; Iglič, A. Mechanical stability of membrane nanotubular protrusions influenced by attachment of flexible rod-like protein. J. Biomech., 2010, 43, 1612-1617.
    • (2010) J. Biomech. , vol.43 , pp. 1612-1617
    • Perutková, S.1    Kralj-Iglič, V.2    Frank, M.3    Iglič, A.4
  • 39
    • 79951502332 scopus 로고    scopus 로고
    • Elastic deformations in hexagonal phases studied by small angle x-ray diffraction and simulations
    • Perutková, S.; Daniel, M.; Rappolt, M.; Pabst, G.; Dolinar, G.; Kralj-Iglič, V.; Iglič, A. Elastic deformations in hexagonal phases studied by small angle x-ray diffraction and simulations. Phys. Chem., 2011, 13, 3100-3107.
    • (2011) Phys. Chem. , vol.13 , pp. 3100-3107
    • Perutková, S.1    Daniel, M.2    Rappolt, M.3    Pabst, G.4    Dolinar, G.5    Kralj-Iglič, V.6    Iglič, A.7
  • 40
    • 77955304814 scopus 로고    scopus 로고
    • Interaction between equally charged membrane surfaces mediated by positively and negatively charged macroions
    • Perutková, S.; Frank, M.; Bohinc, K.; Bobojevič, V.; Rozman, B.; Kralj-Iglič, V.; Iglič, A. Interaction between equally charged membrane surfaces mediated by positively and negatively charged macroions. J. Membr. Biol., 2010, 236, 43-53.
    • (2010) J. Membr. Biol. , vol.236 , pp. 43-53
    • Perutková, S.1    Frank, M.2    Bohinc, K.3    Bobojevič, V.4    Rozman, B.5    Kralj-Iglič, V.6    Iglič, A.7
  • 41
    • 84943997802 scopus 로고
    • Elastic propertiesoflipid bilayers: Theoryand possibleexperiments
    • Helfrich, W. Elastic propertiesoflipid bilayers: theoryand possibleexperiments. Z. Naturforsch. C, 1973, 28, 693-703.
    • (1973) Z. Naturforsch. C , vol.28 , pp. 693-703
    • Helfrich, W.1
  • 42
    • 33845343278 scopus 로고    scopus 로고
    • Quadrupolar ordering of phospholipid molecules in narrow necks of phospholipid vesicles
    • Kralj-Iglič, V.; Babnik, B.; Gauger, D.; May, S.; Iglič, A. Quadrupolar ordering of phospholipid molecules in narrow necks of phospholipid vesicles. J. Stat. Phys., 2006, 125, 727-752.
    • (2006) J. Stat. Phys. , vol.125 , pp. 727-752
    • Kralj-Iglič, V.1    Babnik, B.2    Gauger, D.3    May, S.4    Iglič, A.5
  • 43
    • 33748029142 scopus 로고    scopus 로고
    • Curvature induced accumulation of anisotropic membrane components and raft formation in cylindrical membrane protrusions
    • Iglič, A.; Hägerstrand, H.; Veranič, P.; Plemenitaš, A.; Kralj-Iglič, V.; Curvature induced accumulation of anisotropic membrane components and raft formation in cylindrical membrane protrusions. J. Theor. Biol., 2006, 240, 368-373.
    • (2006) J. Theor. Biol. , vol.240 , pp. 368-373
    • Iglič, A.1    Hägerstrand, H.2    Veranič, P.3    Plemenitaš, A.4    Kralj-Iglič, V.5
  • 44
    • 66249127141 scopus 로고    scopus 로고
    • Sorting of Lipids and Proteins in Membrane Curvature Gradients
    • Tian, A.; Baumgart, T. Sorting of Lipids and Proteins in Membrane Curvature Gradients. Biophys. J., 2009, 96, 2676-2688.
    • (2009) Biophys. J. , vol.96 , pp. 2676-2688
    • Tian, A.1    Baumgart, T.2
  • 46
  • 47
    • 33751218588 scopus 로고    scopus 로고
    • Interaction of giant phospholipid vesicles containing cardiolipin and cholesterol with β2-glycoprotein-I and anti-β2-glycoprotein-I antibodies
    • Ambrožič, A.; Čučnik, S.; Tomšič, N.; Urbanija, J.; Lokar, M.; Babnik, B.; Rozman, B.; Iglič, A.; Kralj-Iglič, V. Interaction of giant phospholipid vesicles containing cardiolipin and cholesterol with β2-glycoprotein-I and anti-β2-glycoprotein-I antibodies. Autoimmun. Rev. 2006, 6, 10-15.
    • (2006) Autoimmun. Rev. , vol.6 , pp. 10-15
    • Ambrožič, A.1    Čučnik, S.2    Tomšič, N.3    Urbanija, J.4    Lokar, M.5    Babnik, B.6    Rozman, B.7    Iglič, A.8    Kralj-Iglič, V.9
  • 51
    • 0028381539 scopus 로고
    • Sensing discrete streptavidinbiotin interactions with atomic force microscopy
    • Lee, G.; Kidwell, D.; Colton, R. Sensing discrete streptavidinbiotin interactions with atomic force microscopy. Langmuir, 1994, 10, 354-357.
    • (1994) Langmuir , vol.10 , pp. 354-357
    • Lee, G.1    Kidwell, D.2    Colton, R.3
  • 52
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy, V.; Florin, E.; Gaub, H. Intermolecular forces and energies between ligands and receptors. Science, 1994, 266, 257-259.
    • (1994) Science , vol.266 , pp. 257-259
    • Moy, V.1    Florin, E.2    Gaub, H.3
  • 53
    • 0032514687 scopus 로고    scopus 로고
    • Forcemediated kinetics of single P selectin/ligand complexes observed by atomic force microscopy
    • Fritz, J.; Katopodis, A.; Kolbinger, F.; Anselmetti, D. Forcemediated kinetics of single P selectin/ligand complexes observed by atomic force microscopy. Proc. Natl. Acad. Sci. USA, 1998, 95, 12283-12288.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12283-12288
    • Fritz, J.1    Katopodis, A.2    Kolbinger, F.3    Anselmetti, D.4
  • 55
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman, K.; Nagy, A. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat. Methods, 2008, 5, 491-505.
    • (2008) Nat. Methods , vol.5 , pp. 491-505
    • Neuman, K.1    Nagy, A.2
  • 56
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating Ligand and Inhibitor Interactions of a Single Antiporter
    • Kedrov, A.; Ziegler, C.; Muller, D. Differentiating Ligand and Inhibitor Interactions of a Single Antiporter. J. Mol. Biol., 2006, 362, 925-932.
    • (2006) J. Mol. Biol. , vol.362 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.3
  • 57
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E.; Ritchie, K. Dynamic strength of molecular adhesion bonds. Biophys. J., 1997, 72, 1541-1555.
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 58
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans, E.; Calderwood, D. Forces and bond dynamics in cell adhesion. Science, 2007, 316, 1148-1153.
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.1    Calderwood, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.