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Volumn 1838, Issue 10, 2014, Pages 2380-2390

Dynamic membrane structure induces temporal pattern formation

Author keywords

Myristoylated electrostatic switch; Temporal pattern formation

Indexed keywords

MARCKS PROTEIN; PROTEIN KINASE C;

EID: 84903399695     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.05.018     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 0017945764 scopus 로고
    • Polymorphism of phospholipid monolayers
    • O. Albrecht, H. Gruler, and E. Sackmann Polymorphism of phospholipid monolayers J. Phys. Fr. 39 3 1978 301 313
    • (1978) J. Phys. Fr. , vol.39 , Issue.3 , pp. 301-313
    • Albrecht, O.1    Gruler, H.2    Sackmann, E.3
  • 2
    • 79951847348 scopus 로고    scopus 로고
    • Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C
    • S. Alonso, U. Dietrich, C. Händel, J.A. Käs, and M. Bär Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C Biophys. J. 100 2011 939 947
    • (2011) Biophys. J. , vol.100 , pp. 939-947
    • Alonso, S.1    Dietrich, U.2    Händel, C.3    Käs, J.A.4    Bär, M.5
  • 3
    • 0030869425 scopus 로고    scopus 로고
    • Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin
    • DOI 10.1074/jbc.272.43.27167
    • A. Arbuzova, J. Wang, D. Murray, J. Jacob, D.S. Cafiso, and S. McLaughlin Kinetics of interaction of the myristoylated alanine-rich c kinase substrate, membranes, and calmodulin J. Biol. Chem. 272 1997 27167 27177 (Pubitemid 27452675)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 27167-27177
    • Arbuzova, A.1    Wang, J.2    Murray, D.3    Jacob, J.4    Cafiso, D.S.5    McLaughlin, S.6
  • 5
    • 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
    • DOI 10.1021/bi001039j
    • A. Arbuzova, L. Wang, J. Wang, G. Hangyás-Milháyné, D. Murray, B. Honig, and S. McLaughlin 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 Biochem. J. 39 2000 10330 10339 (Pubitemid 30665202)
    • (2000) Biochemistry , vol.39 , Issue.33 , 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
  • 6
    • 0037083896 scopus 로고    scopus 로고
    • Cross-talk unfolded: MARCKS proteins
    • DOI 10.1042/0264-6021:3620001
    • A. Arbuzova, A.A.P. Schmitz, and G. Vergères Cross talk unfolded: MARCKS proteins Biochem. J. 362 2002 1 12 (Pubitemid 34174456)
    • (2002) Biochemical Journal , vol.362 , Issue.1 , pp. 1-12
    • Arbuzova, A.1    Schmitz, A.A.P.2    Vergeres, G.3
  • 7
    • 0024219844 scopus 로고
    • Cytosolic calcium oscillators
    • M.J. Berridge, and A. Galione Cytosolic calcium oscillators FASEB J. 2 1988 3074 3082
    • (1988) FASEB J. , vol.2 , pp. 3074-3082
    • Berridge, M.J.1    Galione, A.2
  • 8
    • 0018795945 scopus 로고
    • A comparative study of the phase transitions of phospholipid bilayers and monolayers
    • A. Blume A comparative study of the phase transitions of phospholipid bilayers and monolayers Biochim. Biophys. Acta 557 1979 32 44
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 32-44
    • Blume, A.1
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • E.A. Clark, and J.S. Brugge Integrins and signal transduction pathways: the road taken Science 2680 5208 1995 233 239
    • (1995) Science , vol.2680 , Issue.5208 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 10
    • 0031037109 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate specifically stimulates pp60(c-src) catalyzed phosphorylation of gelsolin and related actin-binding proteins
    • DOI 10.1016/S0014-5793(96)01471-8, PII S0014579396014718
    • V. de Corte, J. Gettemans, and J. Vandekerckhove Phosphatidylinositol 4,5-bisphosphate specifically stimulates PP60c-src catalyzed phosphorylation of gelsolin and related actin-binding proteins FEBS Lett. 401 1997 191 196 (Pubitemid 27056114)
    • (1997) FEBS Letters , vol.401 , Issue.2-3 , pp. 191-196
    • De Corte, V.1    Gettemans, J.2    Vandekerckhove, J.3
  • 12
    • 79957788715 scopus 로고    scopus 로고
    • Structural investigation on the adsorption of the MARCKS peptide on anionic lipid monolayers - Effects beyond electrostatic
    • U. Dietrich, P. Krueger, and J.A. Kaes Structural investigation on the adsorption of the MARCKS peptide on anionic lipid monolayers - effects beyond electrostatic Chem. Phys. Lipids 164 2011 266 275
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 266-275
    • Dietrich, U.1    Krueger, P.2    Kaes, J.A.3
  • 13
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • DOI 10.1038/31960
    • R.E. Dolmetsch, K. Xu, and R.S. Lewis Calciumoscillations increase the efficiency and specificity of gene expression Nature 392 1998 933 936 (Pubitemid 28232066)
    • (1998) Nature , vol.392 , Issue.6679 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 14
    • 43149114463 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy
    • D.R. Dries, and A.C. Newton Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy J. Biol. Chem. 283 2008 7885 7893
    • (2008) J. Biol. Chem. , vol.283 , pp. 7885-7893
    • Dries, D.R.1    Newton, A.C.2
  • 15
    • 43149104977 scopus 로고    scopus 로고
    • Comparing experimental and simulated pressure-area isotherms for DPPC
    • S.L. Duncan, and R.G. Larson Comparing experimental and simulated pressure-area isotherms for DPPC Biophys. J. 94 2008 2965 2986
    • (2008) Biophys. J. , vol.94 , pp. 2965-2986
    • Duncan, S.L.1    Larson, R.G.2
  • 16
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • DOI 10.1038/nature04394
    • D.M. Engelman Membranes are more mosaic than fluid Nature 438 2005 578 580 (Pubitemid 41740560)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 578-580
    • Engelman, D.M.1
  • 17
    • 34147128541 scopus 로고    scopus 로고
    • Reactive boundary conditions for stochastic simulations of reaction-diffusion processes
    • DOI 10.1088/1478-3975/4/1/003, PII S1478397507386342, 003
    • R. Erban, and S.J. Chapman Reactive boundary conditions for stochastic simulations of reaction-diffusion processes Phys. Biol. 4 2007 16 28 (Pubitemid 46553674)
    • (2007) Physical Biology , vol.4 , Issue.1 , pp. 16-28
    • Erban, R.1    Chapman, S.J.2
  • 18
    • 24944487311 scopus 로고    scopus 로고
    • MARCKS is a major PKC-dependent regulator of calmodulin targeting in smooth muscle
    • DOI 10.1242/jcs.02493
    • C. Gallant, J.Y. You, Y. Sasaki, Z. Grabarek, and K.G. Morgan MARCKS is a major PKC-dependent regulator of calmodulin targeting in smooth muscle J. Cell Sci. 180 16 2005 3595 3605 (Pubitemid 41309407)
    • (2005) Journal of Cell Science , vol.118 , Issue.16 , pp. 3595-3605
    • Gallant, C.1    You, J.Y.2    Sasaki, Y.3    Grabarek, Z.4    Morgan, K.G.5
  • 19
    • 0015454185 scopus 로고
    • A theory of biological pattern formation
    • A. Gierer, and H. Meinhardt A theory of biological pattern formation Kybernetik 12 1972 30 39
    • (1972) Kybernetik , vol.12 , pp. 30-39
    • Gierer, A.1    Meinhardt, H.2
  • 21
    • 0024438997 scopus 로고
    • Myristoylated and nonmyristoylated forms of a protein are phosphorylated by protein kinase C
    • J.M. Graff, J.I. Gordon, and P.J. Blackshear Myristoylated and nonmyristoylated forms of a protein are phosphorylated by protein kinase C Science 246 1989 503 506 (Pubitemid 19273942)
    • (1989) Science , vol.246 , Issue.4929 , pp. 503-506
    • Graff, J.M.1    Gordon, J.I.2    Blackshear, P.J.3
  • 22
    • 0026352185 scopus 로고
    • Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
    • J.M. Graff, R.R. Rajan, R.R. Randall, A.C. Nairn, and P.J. Blackshear Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain J. Biol. Chem. 266 1991 14390 14398 (Pubitemid 21907514)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.22 , pp. 14390-14398
    • Graff, J.M.1    Rajan, R.R.2    Randall, R.R.3    Nairn, A.C.4    Blackshear, P.J.5
  • 23
    • 1942455262 scopus 로고    scopus 로고
    • Increased Concentration of Polyvalent Phospholipids in the Adsorption Domain of a Charged Protein
    • E. Haleva, N. Ben-Tal, and H. Diamant Increased concentration of polyvalent phospholipids in the adsorption domain of a charged protein Biophys. J. 86 4 2004 2165 2178 (Pubitemid 38524407)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2165-2178
    • Haleva, E.1    Ben-Tal, N.2    Diamant, H.3
  • 24
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • J.H. Hartwig, M. Thelen, A. Rosen, P.A. Janmey, A.C. Nairn, and A. Aderem MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin Nature 356 1992 618 622
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 25
    • 0037357714 scopus 로고    scopus 로고
    • A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration
    • DOI 10.1021/bp0256059
    • L. He, and B. Niemeyer A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration Biotechnol. Prog. 19 2003 544 548 (Pubitemid 36421008)
    • (2003) Biotechnology Progress , vol.19 , Issue.2 , pp. 544-548
    • He, L.1    Niemeyer, B.2
  • 26
    • 22244481597 scopus 로고    scopus 로고
    • Travelling lipid domains in a dynamic model for protein-induced pattern formation in biomembranes
    • DOI 10.1088/1478-3975/2/2/005
    • K. John, and M. Bär Travelling lipid domains in a dynamic model for protein-induced pattern formation in biomembranes Phys. Biol. 2 2005 123 132 (Pubitemid 40991714)
    • (2005) Physical Biology , vol.2 , Issue.2 , pp. 123-132
    • John, K.1    Bar, M.2
  • 27
    • 0030249769 scopus 로고    scopus 로고
    • Isotherms of dipalmitoylphosphatidylcholine (DPPC) monolayers: Features revealed and features obscured
    • DOI 10.1006/jcis.1996.0454
    • K.J. Klopfer, and T.K. Vanderlick Isotherms of dipalmitoylphosphatidylcholine (DPPC) monolayers: features revealed and features obscured J. Colloid Interface Sci. 182 1996 220 229 (Pubitemid 26305223)
    • (1996) Journal of Colloid and Interface Science , vol.182 , Issue.1 , pp. 220-229
    • Klopfer, K.J.1    Vanderlick, T.K.2
  • 28
    • 77957347061 scopus 로고    scopus 로고
    • Reaction-diffusion model as a framework for understanding biological pattern formation
    • S. Kondo, and T. Miura Reaction-diffusion model as a framework for understanding biological pattern formation Science 329 5999 2010 1616 1620
    • (2010) Science , vol.329 , Issue.5999 , pp. 1616-1620
    • Kondo, S.1    Miura, T.2
  • 29
    • 0034717707 scopus 로고    scopus 로고
    • 2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • DOI 10.1083/jcb.149.7.1455
    • 2 plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism J. Cell Biol. 149 7 2000 1455 1471 (Pubitemid 30437619)
    • (2000) Journal of Cell Biology , vol.149 , Issue.7 , pp. 1455-1471
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 30
    • 0026416651 scopus 로고
    • Spiral calcium wave propagation and annihilation in Xenapus laevis oocytes
    • J. Lechleiter, S. Girard, E. Peralta, and D. Clapham Spiral calcium wave propagation and annihilation in Xenopus laevis oocytes Science 252 1991 123 126 (Pubitemid 21916952)
    • (1991) Science , vol.252 , Issue.5002 , pp. 123-126
    • Lechleiter, J.1    Girard, S.2    Peralta, E.3    Clapham, D.4
  • 31
    • 0025972839 scopus 로고
    • Mechanism of protein kinase C activation by phosphatidylinositol 4,5-bisphosphate
    • M.H. Lee, and R.M. Bell Mechanism of protein kinase C activation by phosphatidylinositol 4,5-bisphosphate Biochem. J. 30 1991 1041 1049
    • (1991) Biochem. J. , vol.30 , pp. 1041-1049
    • Lee, M.H.1    Bell, R.M.2
  • 32
    • 0026629064 scopus 로고
    • Supplementation of the phosphatidyl-L-serine requirement of protein kinase C with nonactivating phospholipids
    • M.H. Lee, and R.M. Bell Supplementation of the phosphatidyl-L-serine requirement of protein kinase C with nonactivating phospholipids Biochem. J. 31 22 1992 5176 5182
    • (1992) Biochem. J. , vol.31 , Issue.22 , pp. 5176-5182
    • Lee, M.H.1    Bell, R.M.2
  • 33
    • 51249114388 scopus 로고    scopus 로고
    • Electrostatic contribution to the surface pressure of charged monolayers containing polyphosphoinositides
    • I. Levental, P.A. Janmey, and A. Cebers Electrostatic contribution to the surface pressure of charged monolayers containing polyphosphoinositides Biophys. J. 95 2008 1199 1205
    • (2008) Biophys. J. , vol.95 , pp. 1199-1205
    • Levental, I.1    Janmey, P.A.2    Cebers, A.3
  • 34
    • 44049091101 scopus 로고    scopus 로고
    • Spatial regulators for bacterial cell division self-organize into surface waves in vitro
    • DOI 10.1126/science.1154413
    • M. Loose, E. Fischer-Friedrich, J. Ries, K. Kruse, and P. Schwille Spatial regulators for bacterial cell division self-organize into surface waves in vitro Science 320 2008 789 792 (Pubitemid 351929626)
    • (2008) Science , vol.320 , Issue.5877 , pp. 789-792
    • Loose, M.1    Fischer-Friedrich, E.2    Ries, J.3    Kruse, K.4    Schwille, P.5
  • 35
    • 0031075965 scopus 로고    scopus 로고
    • On the Induction Criterion of the Marangoni Convection at the Gas/Liquid Interface
    • H.-H. Lu, Y.-M. Yang, and J.-R. Maa On the induction criterion of the marangoni convection at the gas/liquid interface Ind. Eng. Chem. Res. 36 2 1997 474 482 (Pubitemid 127483468)
    • (1997) Industrial and Engineering Chemistry Research , vol.36 , Issue.2 , pp. 474-482
    • Lu, H.-H.1    Yang, Y.-M.2    Maa, J.-R.3
  • 36
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • S. McLaughlin, and A. Aderem The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions Trends Biochem. Sci. 20 1995 272 276
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 38
    • 35448979574 scopus 로고    scopus 로고
    • The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes
    • D. Murray, A. Arbuzova, B. Honig, and S. McLaughlin The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes Curr. Top. Membr. 52 2002 277 307
    • (2002) Curr. Top. Membr. , vol.52 , pp. 277-307
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 39
    • 0035818442 scopus 로고    scopus 로고
    • Membrane binding kinetics of protein kinase C βII mediated by the C2 domain
    • DOI 10.1021/bi010761u
    • E.A. Nalefski, and A.C. Newton Membrane binding kinetics of protein kinase C betaII mediated by the C2 domain Biochem. J. 40 2001 13216 13229 (Pubitemid 33043536)
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13216-13229
    • Nalefski, E.A.1    Newton, A.C.2
  • 40
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Y. Nishizuka Protein kinase C and lipid signaling for sustained cellular responses FASEB J. 9 7 1995 484 496
    • (1995) FASEB J. , vol.9 , Issue.7 , pp. 484-496
    • Nishizuka, Y.1
  • 41
    • 0034713935 scopus 로고    scopus 로고
    • Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate
    • S. Ohmori, N. Sakai, Y. Shirai, H. Yamamoto, E. Miyamoto, N. Shimizu, and N. Saito Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate J. Biol. Chem. 275 2000 26449 26457
    • (2000) J. Biol. Chem. , vol.275 , pp. 26449-26457
    • Ohmori, S.1    Sakai, N.2    Shirai, Y.3    Yamamoto, H.4    Miyamoto, E.5    Shimizu, N.6    Saito, N.7
  • 42
    • 0016302334 scopus 로고
    • Diffusion controlled reaction rates in spheroidal geometry: Application to repressor-operator association and membrane bound enzymes
    • P.H. Richter, and M. Eigen Diffusion controlled reaction rates in spheroidal geometry: application to repressor-operator association and membrane bound enzymes Biophys. Chem. 2 1974 255 263
    • (1974) Biophys. Chem. , vol.2 , pp. 255-263
    • Richter, P.H.1    Eigen, M.2
  • 43
    • 78149419627 scopus 로고    scopus 로고
    • Reaction-diffusion systems in intracellular molecular transport and control
    • S. Soh, M. Byrska, K. Kandere-Grzybowska, and B.A. Grzybowski Reaction-diffusion systems in intracellular molecular transport and control Angew. Chem. 122 2010 4264 4294
    • (2010) Angew. Chem. , vol.122 , pp. 4264-4294
    • Soh, S.1    Byrska, M.2    Kandere-Grzybowska, K.3    Grzybowski, B.A.4
  • 44
    • 0025907984 scopus 로고
    • Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
    • M. Thelen, A. Rosen, A.C. Nairn, and A. Aderem Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane Nature 351 1991 320 322 (Pubitemid 21896590)
    • (1991) Nature , vol.351 , Issue.6324 , pp. 320-322
    • Thelen, M.1    Rosen, A.2    Nairn, A.C.3    Aderem, A.4
  • 47
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-biphosphate
    • J. Wang, A. Arbuzova, G. Hangás-Milháyné, and S. McLaughlin The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-biphosphate J. Biol. Chem. 276 2001 5012 5019
    • (2001) J. Biol. Chem. , vol.276 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangás-Milháyné, G.3    McLaughlin, S.4
  • 48
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-biphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • J. Wang, A. Gambhir, G. Hangyás-Mihályné, D. Murray, U. Golebiewska, and S. McLaughlin Lateral sequestration of phosphatidylinositol 4,5-biphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions J. Biol. Chem. 277 2002 34401 34412
    • (2002) J. Biol. Chem. , vol.277 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    Hangyás-Mihályné, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 49
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
    • F.X. Yu, H.Q. Sun, P.A. Janmey, and H.L. Yin Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin J. Biol. Chem. 267 1992 14616 14621
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmey, P.A.3    Yin, H.L.4


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