메뉴 건너뛰기




Volumn 86, Issue 4, 2004, Pages 2188-2207

Electrostatic Sequestration of PIP2 on Phospholipid Membranes by Basic/Aromatic Regions of Proteins

Author keywords

[No Author keywords available]

Indexed keywords

MARCKS PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHATIDYLSERINE; PHOSPHOLIPASE C; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN KINASE C; LIPOPROTEIN; MEMBRANE PROTEIN; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SIGNAL PEPTIDE;

EID: 1942519695     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74278-2     Document Type: Article
Times cited : (265)

References (109)
  • 1
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem, A. 1992. The MARCKS brothers: a family of protein kinase C substrates. Cell. 71:713-716.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 2
    • 0029752766 scopus 로고    scopus 로고
    • Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope
    • Akashi, K., H. Miyata, H. Itoh, and K. Kinosita, Jr. 1996. Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope. Biophys. J. 71:3242-3250.
    • (1996) Biophys. J. , vol.71 , pp. 3242-3250
    • Akashi, K.1    Miyata, H.2    Itoh, H.3    Kinosita Jr., K.4
  • 3
    • 0023425086 scopus 로고
    • The 87-kDa protein, a major specific substrate for protein kinase C: Purification from bovine brain and characterization
    • Albert, K. A., A. C. Naim, and P. Greengard. 1987. The 87-kDa protein, a major specific substrate for protein kinase C: purification from bovine brain and characterization. Proc. Natl. Acad. Sci. USA. 84:7046-7050.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7046-7050
    • Albert, K.A.1    Naim, A.C.2    Greengard, P.3
  • 4
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages
    • Allen, L. A., and A. Aderem. 1995. A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages. J. Exp. Med. 182:829-840.
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.A.1    Aderem, A.2
  • 6
    • 0031795796 scopus 로고    scopus 로고
    • MARCKS, membranes, and calmodulin: Kinetics of their interaction
    • Arbuzova, A., D. Murray, and S. McLaughlin. 1998. MARCKS, membranes, and calmodulin: kinetics of their interaction. Biochim. Biophys. Acta. 1376:369-379.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 369-379
    • Arbuzova, A.1    Murray, D.2    McLaughlin, S.3
  • 8
    • 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. 2000b. 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
  • 10
    • 0037177352 scopus 로고    scopus 로고
    • Visualizing Cellular Phosphoinositide Pools with GFP-Fused Protein-Modules
    • 2002/125/p13
    • Balla, T., and P. Varnai. 2002. Visualizing Cellular Phosphoinositide Pools with GFP-Fused Protein-Modules. STKE (http://www.stke.org/cgi/content/full/OC_sigtrans); 2002/125/p13:1-16.
    • (2002) STKE , pp. 1-16
    • Balla, T.1    Varnai, P.2
  • 11
    • 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
  • 12
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney, C., and G. Danuser. 2003. FRET or no FRET: a quantitative comparison. Biophys. J. 84:3992-4010.
    • (2003) Biophys. J. , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 14
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge, M. J., and R. F. Irvine. 1984. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature. 312:315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 15
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of alpha-helices with lipid bilayers: A review of simulation studies
    • Biggin, P. C., and M. S. Sansom. 1999. Interactions of alpha-helices with lipid bilayers: a review of simulation studies. Biophys. Chem. 76:161-183.
    • (1999) Biophys. Chem. , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.2
  • 16
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the trojan peptide penetratin across lipids membranes
    • Binder, H., and G. Lindblom. 2003. Charge-dependent translocation of the trojan peptide penetratin across lipids membranes. Biophys. J. 85:982-995.
    • (2003) Biophys. J. , vol.85 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 17
    • 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
  • 20
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D. A., and E. London. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275:17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 21
    • 0027389279 scopus 로고
    • Comparison of the levels of inositol metabolites in transformed heamopoietic cells and their normal counterparts
    • Bunce, C. M., P. H. French, P. Allen, J. C. Mountford, B. Moor, M. F. Greaves, R. H. Michell, and G. Brown. 1993. Comparison of the levels of inositol metabolites in transformed heamopoietic cells and their normal counterparts. Biochem. J. 289:667-673.
    • (1993) Biochem. J. , vol.289 , pp. 667-673
    • Bunce, C.M.1    French, P.H.2    Allen, P.3    Mountford, J.C.4    Moor, B.5    Greaves, M.F.6    Michell, R.H.7    Brown, G.8
  • 22
    • 0034009390 scopus 로고    scopus 로고
    • Signal transduction: Hanging on a scaffold
    • Burack, W. R., and A. S. Shaw. 2000. Signal transduction: hanging on a scaffold. Curr. Opin. Cell Biol. 12:211-216.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 211-216
    • Burack, W.R.1    Shaw, A.S.2
  • 23
    • 0031614308 scopus 로고    scopus 로고
    • Ultracentrifugation technique for measuring the binding of peptides and proteins to sucrose-loaded phospholipid vesicles
    • Buser, C. A., and S. McLaughlin. 1998. Ultracentrifugation technique for measuring the binding of peptides and proteins to sucrose-loaded phospholipid vesicles. Methods Mol. Biol. 84:267-281.
    • (1998) Methods Mol. Biol. , vol.84 , pp. 267-281
    • Buser, C.A.1    McLaughlin, S.2
  • 25
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C. 2002. The phosphoinositide 3-kinase pathway. Science. 296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 26
    • 0035881755 scopus 로고    scopus 로고
    • 2 rafts
    • 2 rafts. EMBO J. 20:4332-4336.
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 27
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona, O., and P. De Camilli. 2001. Phosphoinositides in membrane traffic at the synapse. J. Cell Sci. 114:1041-1052.
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 29
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech, M. P. 2003. Dynamics of phosphoinositides in membrane retrieval and insertion. Annu. Rev. Physiol. 65:791-815.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 30
    • 0032522719 scopus 로고    scopus 로고
    • Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4,5-bisphosphate
    • Dell'Acqua, M. L., M. C. Faux, J. Thorburn, A. Thorburn, and J. D. Scott. 1998. Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4,5-bisphosphate. EMBO J. 17:2246-2260.
    • (1998) EMBO J. , vol.17 , pp. 2246-2260
    • Dell'Acqua, M.L.1    Faux, M.C.2    Thorburn, J.3    Thorburn, A.4    Scott, J.D.5
  • 32
    • 0038603841 scopus 로고    scopus 로고
    • Membrane ruffling requires coordination between Type Iα phosphatidylinositol phosphate kinase and Rac signaling
    • Doughman, R. L., A. J. Firestone, M. L. Wojtasiak, M. W. Bunce, and R. A. Anderson. 2003a. Membrane ruffling requires coordination between Type Iα phosphatidylinositol phosphate kinase and Rac signaling. J. Biol. Chem. 278:23036-23045.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23036-23045
    • Doughman, R.L.1    Firestone, A.J.2    Wojtasiak, M.L.3    Bunce, M.W.4    Anderson, R.A.5
  • 34
    • 0038557037 scopus 로고    scopus 로고
    • Lipids on the frontier: A century of cell-membrane bilayers
    • Edidin, M. 2003. Lipids on the frontier: a century of cell-membrane bilayers. Nat. Rev. Mol. Cell Biol. 4:414-418.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 414-418
    • Edidin, M.1
  • 35
    • 0034057087 scopus 로고    scopus 로고
    • A-kinase anchoring proteins: Protein kinase A and beyond
    • Edwards, A. S., and J. D. Scott. 2000. A-kinase anchoring proteins: protein kinase A and beyond. Curr. Opin. Cell Biol. 12:217-221.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 217-221
    • Edwards, A.S.1    Scott, J.D.2
  • 36
    • 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
  • 37
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D. M., T. A. Steitz, and A. Goldman. 1986. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15:321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 38
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K. M., M. A. Lemmon, J. Schlessinger, and P. B. Sigler. 1995. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell. 83:1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 39
    • 0021257305 scopus 로고
    • Phosphoinositide metabolism and the morphology of human erythrocytes
    • Ferrell, J. E., and W. H. Huestis. 1984. Phosphoinositide metabolism and the morphology of human erythrocytes. J. Cell Biol. 98:1992-1998.
    • (1984) J. Cell Biol. , vol.98 , pp. 1992-1998
    • Ferrell, J.E.1    Huestis, W.H.2
  • 40
    • 0031872177 scopus 로고    scopus 로고
    • Electrostatic contributions to heat capacity changes of DNA-ligand binding
    • Gallagher, K., and K. A. Sharp. 1998. Electrostatic contributions to heat capacity changes of DNA-ligand binding. Biophys. J. 75:769-776.
    • (1998) Biophys. J. , vol.75 , pp. 769-776
    • Gallagher, K.1    Sharp, K.A.2
  • 42
    • 0036674955 scopus 로고    scopus 로고
    • The role of SSeCKS/gravin/AKAP12 scaffolding proteins in the spaciotemporal control of signaling pathways in oncogenesis and development
    • Gelman, I. H. 2002. The role of SSeCKS/gravin/AKAP12 scaffolding proteins in the spaciotemporal control of signaling pathways in oncogenesis and development. Front. Biosci. 7:d1782-d1797.
    • (2002) Front. Biosci. , vol.7
    • Gelman, I.H.1
  • 43
    • 0008678659 scopus 로고    scopus 로고
    • Electric field effects in mulitcomponent fluid lipid membranes
    • Groves, J. R., S. G. Boxer, and H. M. McConnell. 2000. Electric field effects in mulitcomponent fluid lipid membranes. Phys. Chem. B. 104:119-124.
    • (2000) Phys. Chem. B , vol.104 , pp. 119-124
    • Groves, J.R.1    Boxer, S.G.2    McConnell, H.M.3
  • 44
    • 0025173015 scopus 로고
    • Restricted diffusion of integral membrane proteins and polyphosphoinositides leads to their depletion in microvesicles released from human erythrocytes
    • Hagelberg, C., and D. Allan. 1990. Restricted diffusion of integral membrane proteins and polyphosphoinositides leads to their depletion in microvesicles released from human erythrocytes. Biochem. J. 271:831-834.
    • (1990) Biochem. J. , vol.271 , pp. 831-834
    • Hagelberg, C.1    Allan, D.2
  • 45
    • 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. 2003. Increased concentration of polyvalent phospholipids in the adsorption domain of a charged protein. Biophys. J. 86:2165-2178.
    • (2003) Biophys. J. , vol.86 , pp. 2165-2178
    • Haleva, E.1    Ben-Tal, N.2    Diamant, H.3
  • 46
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J. E., P. J. Hajduk, H. S. Yoon, and S. W. Fesik. 1994. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature. 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 47
    • 0035808040 scopus 로고    scopus 로고
    • 2 with Ion Channels and Transporters
    • 2001/111/re19
    • 2 with Ion Channels and Transporters. STKE (http://www.stke.org/cgi/content/full/OC_sigtrans); 2001/111/re19:1-8.
    • (2001) STKE , pp. 1-8
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 49
    • 0037141219 scopus 로고    scopus 로고
    • Coexisting liquid phases in lipid monolayers and bilayers
    • Keller, S. 2002. Coexisting liquid phases in lipid monolayers and bilayers. Journal of Physics: Condensed Matter. 14:4763-4766.
    • (2002) Journal of Physics: Condensed Matter , vol.14 , pp. 4763-4766
    • Keller, S.1
  • 50
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim, J., T. Shishido, X. 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.1    Shishido, T.2    Jiang, X.3    Aderem, A.4    McLaughlin, S.5
  • 53
    • 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
  • 54
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M. A., K. M. Ferguson, R. O'Brien, P. B. Sigler, and J. Schlessinger. 1995. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl. Acad. Sci. USA. 92:10472-10476.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 55
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim, W. A. 2002. The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12:61-68.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 57
    • 0035954430 scopus 로고    scopus 로고
    • Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fcγ receptor-mediated phagocytosis
    • Marshall, J. G., J. W. Booth, V. Stambolic, T. Mak, T. Balla, A. D. Schreiber, T. Meyer, and S. Grinstein. 2001. Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fcγ receptor-mediated phagocytosis. J. Cell Biol. 153:1369-1380.
    • (2001) J. Cell Biol. , vol.153 , pp. 1369-1380
    • Marshall, J.G.1    Booth, J.W.2    Stambolic, V.3    Mak, T.4    Balla, T.5    Schreiber, A.D.6    Meyer, T.7    Grinstein, S.8
  • 58
    • 0035424240 scopus 로고    scopus 로고
    • 2 regulation of surface membrane traffic
    • 2 regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13:493-499.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 60
    • 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
  • 61
    • 0041821501 scopus 로고    scopus 로고
    • Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts
    • McIntosh, T. J., A. Vidal, and S. A. Simon. 2003. Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts. Biophys. J. 85:1656-1666.
    • (2003) Biophys. J. , vol.85 , pp. 1656-1666
    • McIntosh, T.J.1    Vidal, A.2    Simon, S.A.3
  • 62
    • 77957067380 scopus 로고
    • Electrostatic potentials at membrane-solution interfaces
    • McLaughlin, S. 1977. Electrostatic potentials at membrane-solution interfaces. Current Topics in Membranes and Transport. 9:71-144.
    • (1977) Current Topics in Membranes and Transport , vol.9 , pp. 71-144
    • McLaughlin, S.1
  • 64
    • 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
  • 66
    • 0023013610 scopus 로고
    • Separation of phosphoinositides and other phospholipids by two-dimensional thin-layer chromatography
    • Mitchell, K. T., J. E. Ferrell, Jr., and W. H. Huestis. 1986. Separation of phosphoinositides and other phospholipids by two-dimensional thin-layer chromatography. Anal. Biochem. 158:447-453.
    • (1986) Anal. Biochem. , vol.158 , pp. 447-453
    • Mitchell, K.T.1    Ferrell Jr., J.E.2    Huestis, W.H.3
  • 67
    • 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
  • 68
    • 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
  • 69
    • 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
  • 70
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbon
    • Nicholls, A., K. A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbon. Proteins. 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 71
    • 0034713935 scopus 로고    scopus 로고
    • Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate
    • Ohmori, S., N. Sakai, Y. Shira, H. Yamamoto, E. Miyamoto, N. Shimizu, and N. Saito. 2000. Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate. J. Biol. Chem. 275:26449-26457.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26449-26457
    • Ohmori, S.1    Sakai, N.2    Shira, Y.3    Yamamoto, H.4    Miyamoto, E.5    Shimizu, N.6    Saito, N.7
  • 72
    • 0034772748 scopus 로고    scopus 로고
    • Phosphoinositides as key regulators of synaptic function
    • Osborne, S. L., F. A. Meunier, and G. Schiavo. 2001. Phosphoinositides as key regulators of synaptic function. Neuron. 32:9-12.
    • (2001) Neuron , vol.32 , pp. 9-12
    • Osborne, S.L.1    Meunier, F.A.2    Schiavo, G.3
  • 73
    • 0014481138 scopus 로고
    • Energy of an ion crossing a low dielectric membrane: Solutions to four relevant electrostatic problems
    • Parsegian, A. 1969. Energy of an ion crossing a low dielectric membrane: solutions to four relevant electrostatic problems. Nature. 221:844-846.
    • (1969) Nature , vol.221 , pp. 844-846
    • Parsegian, A.1
  • 75
    • 0028954965 scopus 로고
    • Calculations of the electrostatic potential adjacent to model phospholipid bilayers
    • Peitzsch, R. M., M. Eisenberg, K. A. Sharp, and S. McLaughlin. 1995. Calculations of the electrostatic potential adjacent to model phospholipid bilayers. Biophys. J. 68:729-738.
    • (1995) Biophys. J. , vol.68 , pp. 729-738
    • Peitzsch, R.M.1    Eisenberg, M.2    Sharp, K.A.3    McLaughlin, S.4
  • 77
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • Pike, L. J., and J. M. Miller. 1998. Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J. Biol. Chem. 273:22298-22304.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 78
    • 0037799198 scopus 로고    scopus 로고
    • 2 binding site as a determinant of capsaicin receptor sensitivity
    • 2 binding site as a determinant of capsaicin receptor sensitivity. Science. 300:1284-1288.
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 79
    • 0029921472 scopus 로고    scopus 로고
    • Membrane structure of the 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 the 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
  • 80
    • 0032816939 scopus 로고    scopus 로고
    • Condensed complexes of cholesterol and phospholipids
    • Radhakrishnan, A., and H. M. McConnell. 1999. Condensed complexes of cholesterol and phospholipids. Biophys. J. 77:1507-1517.
    • (1999) Biophys. J. , vol.77 , pp. 1507-1517
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 81
    • 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
  • 82
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher, D., T. Stauffer, W. Chen, K. Shen, S. Guo, J. D. York, M. P. Sheetz, and T. Meyer. 2000. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell. 100:221-228.
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 83
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi, M. J., and S. N. Pentyala. 2000. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80:1291-1335.
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 84
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee, S. G. 2001. Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 70:281-312.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 85
    • 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
  • 86
    • 0024203954 scopus 로고
    • 2H and 31P NMR study of pentalysine interaction with headgroup deuterated phosphatidylcholine and phosphatidylserine
    • Roux, M., J. M. Neumann, M. Bloom, and P. F. Devaux. 1988. 2H and 31P NMR study of pentalysine interaction with headgroup deuterated phosphatidylcholine and phosphatidylserine. Eur. Biophys. J. 16:267-273.
    • (1988) Eur. Biophys. J. , vol.16 , pp. 267-273
    • Roux, M.1    Neumann, J.M.2    Bloom, M.3    Devaux, P.F.4
  • 88
    • 0001964325 scopus 로고    scopus 로고
    • Regulation of phospholipase D signaling by phosphoinositides
    • S. Cockcroft, editor. Oxford University Press, Oxford, UK
    • Sciorra, V. A., M. A. Frohman, and A. J. Morris. 2000. Regulation of phospholipase D signaling by phosphoinositides. In Biology of Phosphoinositides. S. Cockcroft, editor. Oxford University Press, Oxford, UK.
    • (2000) Biology of Phosphoinositides
    • Sciorra, V.A.1    Frohman, M.A.2    Morris, A.J.3
  • 89
    • 12444270914 scopus 로고    scopus 로고
    • Experimental and computational studies of the interactions of amphipathic peptides with lipid surfaces
    • S. A. Simon and T. J. McIntosh, editors. Academic Press, San Diego, CA
    • Segrest, J. P., M. A. Jones, V. K. Mishra, and G. M. Anantharamaiah. 2002. Experimental and computational studies of the interactions of amphipathic peptides with lipid surfaces. In Peptide-Lipid Interactions. S. A. Simon and T. J. McIntosh, editors. Academic Press, San Diego, CA. 397-435.
    • (2002) Peptide-Lipid Interactions , pp. 397-435
    • Segrest, J.P.1    Jones, M.A.2    Mishra, V.K.3    Anantharamaiah, G.M.4
  • 90
    • 0037429735 scopus 로고    scopus 로고
    • Role of cholesterol in lipid raft formation: Lessons from lipid model systems
    • Silvius, J. R. 2003. Role of cholesterol in lipid raft formation: lessons from lipid model systems. Biochim. Biophys. Acta. 1610:174-183.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 174-183
    • Silvius, J.R.1
  • 93
    • 0001606761 scopus 로고
    • Interfacial solutions of the Poisson-Boltzmann equation
    • Stillinger, F. H. 1961. Interfacial solutions of the Poisson-Boltzmann equation. J. Chem. Phys. 35:1584-1589.
    • (1961) J. Chem. Phys. , vol.35 , pp. 1584-1589
    • Stillinger, F.H.1
  • 94
    • 0037062590 scopus 로고    scopus 로고
    • Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides
    • Strandberg, E., S. Morein, D. T. Rijkers, R. M. Liskamp, P. C. van der Wel, and J. A. Killian. 2002. Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry. 41:7190-7198.
    • (2002) Biochemistry , vol.41 , pp. 7190-7198
    • Strandberg, E.1    Morein, S.2    Rijkers, D.T.3    Liskamp, R.M.4    Van Der Wel, P.C.5    Killian, J.A.6
  • 95
    • 0029053995 scopus 로고
    • Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions
    • Swierczynski, S. L., and P. J. Blackshear. 1995. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions. J. Biol. Chem. 270:13436-13445.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13436-13445
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 96
    • 0034659468 scopus 로고    scopus 로고
    • Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-supported structures
    • Tall, E., I. Spector, S. N. Pentyala, I. Bitter, and M. J. Rebecchi. 2000. Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-supported structures. Curr. Biol. 10:743-746.
    • (2000) Curr. Biol. , vol.10 , pp. 743-746
    • Tall, E.1    Spector, I.2    Pentyala, S.N.3    Bitter, I.4    Rebecchi, M.J.5
  • 100
    • 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
  • 101
    • 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
  • 102
    • 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
  • 104
    • 0001363220 scopus 로고
    • The phospholipid composition of mammalian tissues
    • R. M. C. Dawson, J. N. Hawthorne, and G. B. Ansell, editors. Elsevier Scientific Publishing Company, Amsterdam, The Netherlands
    • White, D. A. 1973. The phospholipid composition of mammalian tissues. In Form and Function of Phospholipids. R. M. C. Dawson, J. N. Hawthorne, and G. B. Ansell, editors. Elsevier Scientific Publishing Company, Amsterdam, The Netherlands. 441-78.
    • (1973) Form and Function of Phospholipids , pp. 441-478
    • White, D.A.1
  • 105
    • 0030589612 scopus 로고    scopus 로고
    • Structural views of phosphoinositide-specific phospholipase C: Signalling the way ahead
    • Williams, R. L., and M. Katan. 1996. Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead. Structure. 4:1387-1394.
    • (1996) Structure , vol.4 , pp. 1387-1394
    • Williams, R.L.1    Katan, M.2
  • 107
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin, H. L., and P. A. Janmey. 2003. Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65:761-789.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 108
    • 0002017229 scopus 로고
    • Biological distribution
    • G. Cevc, editor. Marcel Dekker, New York
    • Yorek, M. A. 1993. Biological distribution. In Phospholipids Handbook. G. Cevc, editor. Marcel Dekker, New York. 745-75.
    • (1993) Phospholipids Handbook , pp. 745-775
    • Yorek, M.A.1
  • 109
    • 0037821876 scopus 로고    scopus 로고
    • Binding of peptides with basic and aromatic residues to bilayer membranes: Phenylalanine in the MARCKS 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 MARCKS 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.