메뉴 건너뛰기




Volumn 86, Issue 4, 2004, Pages 2165-2178

Increased Concentration of Polyvalent Phospholipids in the Adsorption Domain of a Charged Protein

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPID;

EID: 1942455262     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74276-9     Document Type: Article
Times cited : (56)

References (51)
  • 1
    • 84956262382 scopus 로고
    • Phase transitions between vesicles and micelles driven by competing curvatures
    • Andelman, D., M. M. Kozlov, and W. Helfrich. 1994. Phase transitions between vesicles and micelles driven by competing curvatures. Europhys. Lett. 25:231-236.
    • (1994) Europhys. Lett. , vol.25 , pp. 231-236
    • Andelman, D.1    Kozlov, M.M.2    Helfrich, W.3
  • 2
    • 77957042676 scopus 로고
    • Electrostatic properties of membranes: The Poisson Boltzmann theory
    • R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam, The Netherlands
    • Andelman, D. 1995. Electrostatic properties of membranes: the Poisson Boltzmann theory. In Structure and Dynamics of Membranes, 2nd Ed, Vol 1B. R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam, The Netherlands. 603-642.
    • (1995) Structure and Dynamics of Membranes, 2nd Ed. , vol.1 B , pp. 603-642
    • Andelman, D.1
  • 3
    • 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. Hangyas-Mihalyne, D. Murray, B. 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    Hangyas-Mihalyne, G.4    Murray, D.5    Honig, B.6    McLaughlin, S.7
  • 4
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • Ben-Tal, N., B. Honig, R. M. Peitzsch, G. Denisov, and S. McLaughlin. 1996. Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys. J. 71: 561-575.
    • (1996) Biophys. J. , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 5
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal, N., B. Honig, C. Miller, and S. McLaughlin. 1997. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 73:1717-1727.
    • (1997) Biophys. J. , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 6
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear, P. J. 1993. The MARCKS family of cellular protein kinase C substrates. J. Biol. Chem. 268:1501-1504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 7
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: Complex roles at the cell surface
    • Czech, M. P. 2000. PIP2 and PIP3: complex roles at the cell surface. Cell. 100:603-606.
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 8
    • 33645705346 scopus 로고
    • Membrane-induced interactions between inclusions
    • Dan, N., P. Pincus, and S. A. Safran. 1993. Membrane-induced interactions between inclusions. Langmuir. 9:2768-2771.
    • (1993) Langmuir , vol.9 , pp. 2768-2771
    • Dan, N.1    Pincus, P.2    Safran, S.A.3
  • 10
    • 0036213814 scopus 로고    scopus 로고
    • Poisson-Boltzmann theory for membranes with mobile charged lipids and the pH-dependent interaction of a DNA molecule with a membrane
    • Fleck, C., R. R. Netz, and H. H. von Grünberg. 2002. Poisson-Boltzmann theory for membranes with mobile charged lipids and the pH-dependent interaction of a DNA molecule with a membrane. Biophys. J. 82: 76-92.
    • (2002) Biophys. J. , vol.82 , pp. 76-92
    • Fleck, C.1    Netz, R.R.2    Von Grünberg, H.H.3
  • 12
    • 0029066848 scopus 로고
    • Theory of electrostatic interactions in macromolecules
    • Gilson, M. K. 1995. Theory of electrostatic interactions in macromolecules. Curr. Opin. Struct. Biol. 5:216-223.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 216-223
    • Gilson, M.K.1
  • 13
    • 0031471073 scopus 로고    scopus 로고
    • Electric field-induced reorganization of two-component supported bilayer membranes
    • Groves, J. T., S. G. Boxer, and H. M. McConnell. 1997. Electric field-induced reorganization of two-component supported bilayer membranes. Proc. Natl. Acad. Sci. USA. 94:13390-13395.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13390-13395
    • Groves, J.T.1    Boxer, S.G.2    McConnell, H.M.3
  • 14
    • 0032477732 scopus 로고    scopus 로고
    • Electric field-induced critical demixing in lipid bilayer membranes
    • Groves, J. T., S. G. Boxer, and H. M. McConnell. 1998. Electric field-induced critical demixing in lipid bilayer membranes. Proc. Natl. Acad. Sci. USA. 95:935-938.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 935-938
    • Groves, J.T.1    Boxer, S.G.2    McConnell, H.M.3
  • 15
    • 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
  • 16
    • 0033031748 scopus 로고    scopus 로고
    • Binding of peripheral proteins to mixed lipid membranes: Effect of lipid demixing upon binding
    • Heimburg, T., B. Angerstein, and D. Marsh. 1999. Binding of peripheral proteins to mixed lipid membranes: effect of lipid demixing upon binding. Biophys. J. 76:2575-2586.
    • (1999) Biophys. J. , vol.76 , pp. 2575-2586
    • Heimburg, T.1    Angerstein, B.2    Marsh, D.3
  • 17
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • Honig, B., K. Sharp, and A. Suei-Yang. 1993. Macroscopic models of aqueous solutions: biological and chemical applications. J. Phys. Chem. 97:1101-1109.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Suei-Yang, A.3
  • 18
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 19
    • 0001166775 scopus 로고    scopus 로고
    • Phosphoinositide-specific phospholipase C: Structural basis for catalysis and regulatory interactions
    • Katan, M., and R. L. Williams. 1997. Phosphoinositide-specific phospholipase C: structural basis for catalysis and regulatory interactions. Semin. Cell Dev. Biol. 8:287-296.
    • (1997) Semin. Cell Dev. Biol. , vol.8 , pp. 287-296
    • Katan, M.1    Williams, R.L.2
  • 20
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux, T., K. Fukami, M. Thelen, T. Golub, D. Frey, and P. Caroni. 2000. GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J. Cell Biol. 149:1455-1472.
    • (2000) J. Cell Biol. , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 21
    • 0028763696 scopus 로고
    • Electric-field-induced concentration gradients in lipid monolayers
    • Lee, K. Y. C., J. F. Klinger, and H. M. McConnell. 1994. Electric-field-induced concentration gradients in lipid monolayers. Science. 263: 655-658.
    • (1994) Science , vol.263 , pp. 655-658
    • Lee, K.Y.C.1    Klinger, J.F.2    McConnell, H.M.3
  • 22
    • 0028945733 scopus 로고
    • Effect of electric-field gradients on lipid monolayer membranes
    • Lee, K. Y. C., and H. M. McConnell. 1995. Effect of electric-field gradients on lipid monolayer membranes. Biophys. J. 68:1740-1751.
    • (1995) Biophys. J. , vol.68 , pp. 1740-1751
    • Lee, K.Y.C.1    McConnell, H.M.2
  • 23
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon, M. A. 2003. Phosphoinositide recognition domains. Traffic. 4:201-213.
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 24
    • 0032576969 scopus 로고    scopus 로고
    • Compartmentalization of phosphatidlyinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin
    • Liu, Y., L. Casey, and L. J. Pike. 1998. Compartmentalization of phosphatidlyinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin. Biochem. Biophys. Res. Commun. 245:684-690.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 684-690
    • Liu, Y.1    Casey, L.2    Pike, L.J.3
  • 25
    • 0033929093 scopus 로고    scopus 로고
    • Adducin: Structure, function and regulation
    • Matsuoka, Y., X. Li, and V. Bennett. 2000. Adducin: structure, function and regulation. Cell. Mol. Life Sci. 57:884-895.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 884-895
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 26
    • 0033768029 scopus 로고    scopus 로고
    • Theories on structural perturbations of lipid bilayers
    • May, S. 2000. Theories on structural perturbations of lipid bilayers. Curr. Opin. Coll. Interface Sci. 5:244-249.
    • (2000) Curr. Opin. Coll. Interface Sci. , vol.5 , pp. 244-249
    • May, S.1
  • 27
    • 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
  • 28
    • 18744365208 scopus 로고    scopus 로고
    • Macroion-induced compositional instability of binary fluid membranes
    • May, S., D. Harries, and A. Ben-Shaul. 2002. Macroion-induced compositional 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
  • 29
    • 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
  • 31
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray, D., N. Ben-Tal, B. Honig, and S. McLaughlin. 1997. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure. 5:985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 32
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment
    • Murray, D., A. Arbuzova, G. Hangyas-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    Hangyas-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6    McLaughlin, S.7
  • 33
    • 0035977019 scopus 로고    scopus 로고
    • The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers
    • Murray, D., S. McLaughlin, and B. Honig. 2001. The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers. J. Biol. Chem. 276:45153-45159.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45153-45159
    • Murray, D.1    McLaughlin, S.2    Honig, B.3
  • 34
    • 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. 52:271-302.
    • (2002) Curr. Top. Membr. , vol.52 , pp. 271-302
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 35
    • 0036161583 scopus 로고    scopus 로고
    • Electrostatic control of the membrane targeting of C2 domains
    • Murray, D., and B. Honig. 2002. Electrostatic control of the membrane targeting of C2 domains. Mol. Cell. 9:145-154.
    • (2002) Mol. Cell , vol.9 , pp. 145-154
    • Murray, D.1    Honig, B.2
  • 36
    • 0001552389 scopus 로고    scopus 로고
    • Electrostatistics of counter-ions at and between planar charged walls: From Poisson-Boltzmann to the strong-coupling theory
    • Netz, R. R. 2001. Electrostatistics of counter-ions at and between planar charged walls: from Poisson-Boltzmann to the strong-coupling theory. Eur. Phys. J. E. 5:557-574.
    • (2001) Eur. Phys. J. E , vol.5 , pp. 557-574
    • Netz, R.R.1
  • 37
    • 0015396878 scopus 로고
    • On the electrostatic interaction across a salt solution between two bodies bearing unequal charges
    • Parsegian, V. A., and D. Gingell. 1972. On the electrostatic interaction across a salt solution between two bodies bearing unequal charges. Biophys. J. 12:1192-1204.
    • (1972) Biophys. J. , vol.12 , pp. 1192-1204
    • Parsegian, V.A.1    Gingell, D.2
  • 39
    • 0029921472 scopus 로고    scopus 로고
    • Membrane structure of protein kinase C and calmodulin binding domain of myristoylated alanine rich C kinase substrate determined by site-directed spin labeling
    • Qin, Z. and D. S. Cafiso. 1996. Membrane structure of protein kinase C and calmodulin binding domain of myristoylated alanine rich C kinase substrate determined by site-directed spin labeling. Biochemistry. 35:2917-2925.
    • (1996) Biochemistry , vol.35 , pp. 2917-2925
    • Qin, Z.1    Cafiso, D.S.2
  • 40
    • 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. 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.4
  • 41
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta. 1451:1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 42
    • 0033578731 scopus 로고    scopus 로고
    • Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene
    • Rossi, E. A., Z. Li, H. Feng, and C. S. Rubin. 1999. Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene. J. Biol. Chem. 274:27201-27210.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27201-27210
    • Rossi, E.A.1    Li, Z.2    Feng, H.3    Rubin, C.S.4
  • 43
    • 0007425498 scopus 로고    scopus 로고
    • Competitive electrostatic binding of charged ligands to polyelectrolytes: Planar and cylindrical geometries
    • Rouzina, I., and V. A. Bloomfield. 1996. Competitive electrostatic binding of charged ligands to polyelectrolytes: planar and cylindrical geometries. J. Phys. Chem. 100:4292-4304.
    • (1996) J. Phys. Chem. , vol.100 , pp. 4292-4304
    • Rouzina, I.1    Bloomfield, V.A.2
  • 44
    • 0038440695 scopus 로고    scopus 로고
    • The effect of lipid demixing on the electrostatic interaction of planar membranes across a salt solution
    • Russ, C., T. Heimburg, and H. H. von Grünberg. 2003. The effect of lipid demixing on the electrostatic interaction of planar membranes across a salt solution. Biophys. J. 84:3730-3742.
    • (2003) Biophys. J. , vol.84 , pp. 3730-3742
    • Russ, C.1    Heimburg, T.2    Von Grünberg, H.H.3
  • 46
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer, T. P., S. Ahn, and T. Meyer. 1998. Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr. Biol. 8:343-346.
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 47
    • 0024293197 scopus 로고
    • Adsorption of cations to phosphotidylinsitol 4,5-bisphosphate
    • Toner, M., G. Vaio, A. McLaughlin, and S. McLaughlin. 1988. Adsorption of cations to phosphotidylinsitol 4,5-bisphosphate. Biochemistry. 27:7435-7443.
    • (1988) Biochemistry , vol.27 , pp. 7435-7443
    • Toner, M.1    Vaio, G.2    McLaughlin, A.3    McLaughlin, S.4
  • 48
    • 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. Hangyas-Mihalyne, 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    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 49
    • 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., A. Gambhir, G. Hangyas-Mihalyne, 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.1    Gambhir, A.2    Hangyas-Mihalyne, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 51
    • 0037821876 scopus 로고    scopus 로고
    • Binding of peptides with basic and aromatic residues to bilayer membranes: Phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer
    • Zhang, W., E. Crocker, S. McLaughlin, and S. O. Smith. 2003. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. J. Biol. Chem. 278:21459-21466.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21459-21466
    • Zhang, W.1    Crocker, E.2    McLaughlin, S.3    Smith, S.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.