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Volumn 95, Issue 4, 2008, Pages 1745-1757

The "electrostatic-switch" mechanism: Monte Carlo study of MARCKS-membrane interaction

Author keywords

[No Author keywords available]

Indexed keywords

MARCKS PROTEIN; MEMBRANE PROTEIN; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; PHOSPHOLIPID; SIGNAL PEPTIDE;

EID: 50349099769     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.132522     Document Type: Article
Times cited : (40)

References (46)
  • 1
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association of synapsins with synaptic vesicles
    • Hosaka, M., R. E. Hammer, and T. C. Sudhof. 1999. A phospho-switch controls the dynamic association of synapsins with synaptic vesicles. Neuron. 24:377-387.
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Sudhof, T.C.3
  • 2
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane
    • Ono, A., S. D. Ablan, S. J. Lockett, K. Nagashima, and E. O. Freed. 2004. Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. USA. 101:14889-14894.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 3
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem. 1995. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20:272-276.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 5
    • 33845311555 scopus 로고    scopus 로고
    • Tools to tamper with phosphoinositides
    • McLaughlin, S. 2006. Tools to tamper with phosphoinositides. Science. 314:1402-1403.
    • (2006) Science , vol.314 , pp. 1402-1403
    • McLaughlin, S.1
  • 6
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P-3 and PI(4,5)P-2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo, W. D., T. Inoue, W. S. Park, M. L. Kim, B. O. Park, T. J. Wandless, and T. Meyer. 2006. PI(3,4,5)P-3 and PI(4,5)P-2 lipids target proteins with polybasic clusters to the plasma membrane. Science. 314:1458-1461.
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6    Meyer, T.7
  • 7
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung, T., G. E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein. 2008. Membrane phosphatidylserine regulates surface charge and protein localization. Science. 319:210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 9
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate
    • Wang, J., A. Arbuzova, G. Hangyás-Mihályné, and S. McLaughlin. 2001. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 276:5012-5019.
    • (2001) J. Biol. Chem , vol.276 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangyás-Mihályné, G.3    McLaughlin, S.4
  • 14
    • 3543083870 scopus 로고    scopus 로고
    • The coworkers of actin filaments: From cell structures to signals
    • Revenu, C., R. Athman, S. Robine, and D. Louvard. 2004. The coworkers of actin filaments: from cell structures to signals. Nat. Rev. Mol. Cell Biol. 5:1-12.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 1-12
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 15
    • 0037083896 scopus 로고    scopus 로고
    • Cross-talk unfolded: MARCKS proteins. Part 1
    • Arbuzova, A., A. A. P. Schmitz, and G. Vergeres. 2002. Cross-talk unfolded: MARCKS proteins. Part 1. Biochem. J. 362:1-12.
    • (2002) Biochem. J , vol.362 , pp. 1-12
    • Arbuzova, A.1    Schmitz, A.A.P.2    Vergeres, G.3
  • 16
    • 0001704947 scopus 로고    scopus 로고
    • MARCKS regulates membrane ruffling and cell spreading
    • Myat, M. M., S. Anderson, L. H. Allen, and A. Aderem. 1997. MARCKS regulates membrane ruffling and cell spreading. Curr. Biol. 7:611-614.
    • (1997) Curr. Biol , vol.7 , pp. 611-614
    • Myat, M.M.1    Anderson, S.2    Allen, L.H.3    Aderem, A.4
  • 18
    • 35448979574 scopus 로고    scopus 로고
    • The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes
    • Murray, D., A. Arbuzova, B. Honig, and S. McLaughlin. 2002. The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes. Curr. Top. Membr. 52:277-307.
    • (2002) Curr. Top. Membr , vol.52 , pp. 277-307
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 19
    • 27744464849 scopus 로고    scopus 로고
    • Flexible charged macromolecules on mixed fluid lipid membranes: Theory and Monte Carlo simulations
    • Tzlil, S., and A. Ben-Shaul. 2005. Flexible charged macromolecules on mixed fluid lipid membranes: theory and Monte Carlo simulations. Biophys. J. 89:2972-2987.
    • (2005) Biophys. J , vol.89 , pp. 2972-2987
    • Tzlil, S.1    Ben-Shaul, A.2
  • 20
    • 36849137515 scopus 로고
    • Monte Carlo simulations of the average extension of molecular chains
    • Rosenbluth, M. N., and A. W. Rosenbluth. 1955. Monte Carlo simulations of the average extension of molecular chains. J. Chem. Phys. 23:356-359.
    • (1955) J. Chem. Phys , vol.23 , pp. 356-359
    • Rosenbluth, M.N.1    Rosenbluth, A.W.2
  • 22
    • 0031807139 scopus 로고    scopus 로고
    • Structure, stability and thermodynamics of lamellar DNA-lipid complexes
    • Harries, D., S. May, W. M. Gelbart, and A. Ben-Shaul. 1998. Structure, stability and thermodynamics of lamellar DNA-lipid complexes. Biophys. J. 75:159-173.
    • (1998) Biophys. J , vol.75 , pp. 159-173
    • Harries, D.1    May, S.2    Gelbart, W.M.3    Ben-Shaul, A.4
  • 23
    • 0033807597 scopus 로고    scopus 로고
    • Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes
    • May, S., D. Harries, and A. Ben-Shaul. 2000. Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes. Biophys. J. 79:1747-1760.
    • (2000) Biophys. J , vol.79 , pp. 1747-1760
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 24
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment
    • Murray, D., A. Arbuzova, G. Hangys-Mihalyne, A. Gambhir, N. Ben-Tal, B. Honig, and S. McLaughlin. 1999. Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experiment. Biophys. J. 77:3176-3188.
    • (1999) Biophys. J , vol.77 , pp. 3176-3188
    • Murray, D.1    Arbuzova, A.2    Hangys-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6    McLaughlin, S.7
  • 26
    • 18744365208 scopus 로고    scopus 로고
    • Macroion-induced instability of binary fluid membranes
    • May, S., D. Harries, and A. Ben-Shaul. 2002. Macroion-induced instability of binary fluid membranes. Phys. Rev. Lett. 89:268102.
    • (2002) Phys. Rev. Lett , vol.89 , pp. 268102
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 27
    • 21244448091 scopus 로고    scopus 로고
    • Domain formation induced by the adsorption of charged proteins on mixed lipid membranes
    • Mbamala, E. C., A. Ben-Shaul, and S. May. 2005. Domain formation induced by the adsorption of charged proteins on mixed lipid membranes. Biophys. J. 88:1702-1714.
    • (2005) Biophys. J , vol.88 , pp. 1702-1714
    • Mbamala, E.C.1    Ben-Shaul, A.2    May, S.3
  • 28
    • 42149172539 scopus 로고    scopus 로고
    • Matrix formalism for site-specific binding of unstructured proteins to multicomponent lipid membranes
    • Teif, V. B., D. Harries, D. Lando, and A. Ben-Shaul. 2008. Matrix formalism for site-specific binding of unstructured proteins to multicomponent lipid membranes. J. Pept. Sci. 14:368-373.
    • (2008) J. Pept. Sci , vol.14 , pp. 368-373
    • Teif, V.B.1    Harries, D.2    Lando, D.3    Ben-Shaul, A.4
  • 29
    • 4243189532 scopus 로고
    • Electrostatic persistence length of a wormlike polyelectrolyte
    • Skolnick, J., and M. Fixman. 1977. Electrostatic persistence length of a wormlike polyelectrolyte. Macromolecules. 10:944-948.
    • (1977) Macromolecules , vol.10 , pp. 944-948
    • Skolnick, J.1    Fixman, M.2
  • 30
    • 0017468271 scopus 로고
    • Polyelectrolytes near rod limit
    • Odijk, T. 1977. Polyelectrolytes near rod limit. J. Pol. Sci. B Pol. Phys. 15:477-483.
    • (1977) J. Pol. Sci. B Pol. Phys , vol.15 , pp. 477-483
    • Odijk, T.1
  • 31
    • 0141754072 scopus 로고    scopus 로고
    • Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles
    • Ellena, J. F., M. C. Burnitz, and D. S. Cafiso. 2003. Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles. Biophys. J. 85:2442-2448.
    • (2003) Biophys. J , vol.85 , pp. 2442-2448
    • Ellena, J.F.1    Burnitz, M.C.2    Cafiso, D.S.3
  • 32
    • 44849120746 scopus 로고    scopus 로고
    • MARCKS-HUMAN
    • MARCKS-HUMAN. 2007. Swiss-Prot. http://www.expasy.org/uniprot/P29966.
    • (2007) Swiss-Prot
  • 34
    • 0042902812 scopus 로고
    • A new offlattice Monte-Carlo model for polymers - a comparison of static and dynamic properties with the bond-fluctuation model and application to random-media
    • Gerroff, I., A. Milchev, K. Binder, and W. Paul. 1993. A new offlattice Monte-Carlo model for polymers - a comparison of static and dynamic properties with the bond-fluctuation model and application to random-media. J. Chem. Phys. 98:6526-6539.
    • (1993) J. Chem. Phys , vol.98 , pp. 6526-6539
    • Gerroff, I.1    Milchev, A.2    Binder, K.3    Paul, W.4
  • 35
    • 0000364910 scopus 로고    scopus 로고
    • Debye-Huckel theory for interfacial geometries
    • Netz, R. R. 1999. Debye-Huckel theory for interfacial geometries. Phys. Rev. E Stat. 60:3174-3182.
    • (1999) Phys. Rev. E Stat , vol.60 , pp. 3174-3182
    • Netz, R.R.1
  • 36
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 37
    • 1942455262 scopus 로고    scopus 로고
    • Increased concentration of polyvalent phospholipids in the adsorption domain of a charged protein
    • Haleva, E., N. Ben-Tal, and H. Diamant. 2004. Increased concentration of polyvalent phospholipids in the adsorption domain of a charged protein. Biophys. J. 86:2165-2178.
    • (2004) Biophys. J , vol.86 , pp. 2165-2178
    • Haleva, E.1    Ben-Tal, N.2    Diamant, H.3
  • 38
    • 41649099937 scopus 로고    scopus 로고
    • Protein diffusion on charged membranes: A dynamic mean-field model describes time evolution and lipid reorganization
    • Khelashvili, G., H. Weinstein, and D. Harries. 2008. Protein diffusion on charged membranes: a dynamic mean-field model describes time evolution and lipid reorganization. Biophys. J. 94:2580-2597.
    • (2008) Biophys. J , vol.94 , pp. 2580-2597
    • Khelashvili, G.1    Weinstein, H.2    Harries, D.3
  • 39
    • 0037134540 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers
    • Rauch, M. E., C. G. Ferguson, G. D. Prestwich, and D. S. Cafiso. 2002. Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. J. Biol. Chem. 277:14068-14076.
    • (2002) J. Biol. Chem , vol.277 , pp. 14068-14076
    • Rauch, M.E.1    Ferguson, C.G.2    Prestwich, G.D.3    Cafiso, D.S.4
  • 41
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles
    • Rusu, L., A. Gambhir, S. McLaughlin, and J. Rädler. 2004. Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles. Biophys. J. 87:1044-1053.
    • (2004) Biophys. J , vol.87 , pp. 1044-1053
    • Rusu, L.1    Gambhir, A.2    McLaughlin, S.3    Rädler, J.4
  • 42
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic-strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim, J. Y., T. Shishido, X. L. Jiang, A. Aderem, and S. McLaughlin. 1994. Phosphorylation, high ionic-strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 269:28214-28219.
    • (1994) J. Biol. Chem , vol.269 , pp. 28214-28219
    • Kim, J.Y.1    Shishido, T.2    Jiang, X.L.3    Aderem, A.4    McLaughlin, S.5
  • 43
    • 0039182142 scopus 로고    scopus 로고
    • Interactions controlling the membrane binding of basic protein domains: Phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces
    • Victor, K., J. Jacob, and D. S. Cafiso. 1999. Interactions controlling the membrane binding of basic protein domains: Phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces. Biochemistry. 38:12527-12536.
    • (1999) Biochemistry , vol.38 , pp. 12527-12536
    • Victor, K.1    Jacob, J.2    Cafiso, D.S.3
  • 44
    • 0034702838 scopus 로고    scopus 로고
    • Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS
    • Arbuzova, A., L. Wang, J. Wang, G. Hangyás-Mihályné, D. Murray, D. Honig, and S. McLaughlin. 2000. Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. Biochemistry. 39:10330-10339.
    • (2000) Biochemistry , vol.39 , pp. 10330-10339
    • Arbuzova, A.1    Wang, L.2    Wang, J.3    Hangyás-Mihályné, G.4    Murray, D.5    Honig, D.6    McLaughlin, S.7
  • 45
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • Wang, J. Y., A. Gambhir, G. Hangyás-Mihályné, D. Murray, U. Golebiewska, and S. McLaughlin. 2002. Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. J. Biol. Chem. 277:34401-34412.
    • (2002) J. Biol. Chem , vol.277 , pp. 34401-34412
    • Wang, J.Y.1    Gambhir, A.2    Hangyás-Mihályné, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 46
    • 44949238672 scopus 로고    scopus 로고
    • Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cells
    • Golebiewska, U., M. Nyako, W. Woturski, I. Zaitseva, and S. McLaughlin. 2008. Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cells. Mol. Biol. Cell. 19:1663-1669.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1663-1669
    • Golebiewska, U.1    Nyako, M.2    Woturski, W.3    Zaitseva, I.4    McLaughlin, S.5


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