Alternative mechanisms of structuring biomembranes: Self-assembly versus self-organization

Physical Review Letters

Volumn 95, Issue 19, 2005, Pages

  John, Karin ^a   Bär, Markus ^b  

^a MAX PLANCK INSTITUT FÜR PHYSIK KOMPLEXER SYSTEME   (Germany)

^b PHYSIKALISCH TECHNISCHE BUNDESANSTALT   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

LIPID-PROTEIN INTERACTIONS; PROTEIN PATTERNS; SELF-ORGANIZATION;

BIOCHEMISTRY; CELLS; LIPIDS; MATHEMATICAL MODELS; PROTEINS; SELF ASSEMBLY;

BIOLOGICAL MEMBRANES;

MEMBRANE PROTEIN;

ALGORITHM; CELL FUNCTION; CHEMISTRY; MEMBRANE; PARTICLE SIZE; PHOSPHORYLATION; STATISTICAL MODEL;

ALGORITHMS; CELL PHYSIOLOGICAL PHENOMENA; MEMBRANE PROTEINS; MEMBRANES; MODELS, STATISTICAL; PARTICLE SIZE; PHOSPHORYLATION;

EID: 28844507303     PISSN: 00319007     EISSN: 10797114     Source Type: Journal    
DOI: 10.1103/PhysRevLett.95.198101     Document Type: Article

References (32)

1. B. Alberts, Molecular Biology of the Cell (Garland Publishing, London and New York, 1994).
2. C.L. Manahan, Annu. Rev. Cell Dev. Biol. 20, 223 (2004). ARDBF8 1081-0706 10.1146/annurev.cellbio.20.011303.132633
3. T. Misteli, J. Cell Biol. 155, 181 (2001). JCLBA3 0021-9525 10.1083/jcb.200108110
4. S.L. Veatch and S.L. Keller, Phys. Rev. Lett. 89, 268101 (2002). PRLTAO 0031-9007 10.1103/PhysRevLett.89.268101
5. H.M. McConnell and M. Vrljic, Annu. Rev. Biophys. Biomol. Struct. 32, 469 (2003). ABBSE4 1056-8700 10.1146/annurev.biophys.32.110601.141704
6. M. Glaser, J. Biol. Chem. 271, 26187 (1996). JBCHA3 0021-9258 10.1074/jbc.271.42.26187
7. D. Murray, Biophys. J. 77, 3176 (1999). BIOJAU 0006-3495
8. S. May, D. Harries, and A. Ben-Shaul, Phys. Rev. Lett. 89, 268102 (2002). PRLTAO 0031-9007 10.1103/PhysRevLett.89.268102
9. T.G. Anderson and H.M. McConnell, J. Phys. Chem. B JPCBFK 1520-6106 104, 9918 (2000). 10.1021/jp0019355
10. A. Turing, Phil. Trans. R. Soc. B PTRBAE 0962-8436 237, 37 (1952).
11. A. Gierer and H. Meinhardt, Kybernetik 12, 30 (1972). KYBEAP 0023-5946 10.1007/BF00289234
12. M. Falcke, Adv. Phys. 53, 255 (2004). ADPHAH 0001-8732 10.1080/00018730410001703159
13. M. Howard and K. Kruse, J. Cell Biol. 168, 533 (2005). JCLBA3 0021-9525 10.1083/jcb.200411122
14. P.J. Blackshear, J. Biol. Chem. 268, 1501 (1993). JBCHA3 0021-9258
15. S. McLaughlin, Annu. Rev. Biophys. Biomol. Struct. ABBSE4 1056-8700 31, 151 (2002). 10.1146/annurev.biophys.31.082901.134259
16. D. Frey, J. Cell Biol. 149, 1443 (2000). JCLBA3 0021-9525 10.1083/jcb.149.7.1443
17. T. Laux, J. Cell Biol. 149, 1455 (2000). JCLBA3 0021-9525 10.1083/jcb.149.7.1455
18. A. Arbuzova, Biochemistry BICHAW 0144-0578 39, 10330 (2000). 10.1021/bi001039j
19. J. Cahn and J. Hilliard, J. Chem. Phys. 28, 258 (1958). JCPSA6 0021-9606 10.1063/1.1744102
20. M. Thelen, Nature (London) NATUAS 0028-0836 351, 320 (1991). 10.1038/351320a0
21. G.M. Verghese, J. Biol. Chem. 269, 9361 (1994). JBCHA3 0021-9258
22. K. Seki, H.-C. Chen, and K.-P. Huang, Archives of Biochemistry and Biophysics ABBIA4 0003-9861 316, 673 (1995). 10.1006/abbi.1995.1090
23. Biology of Phosphoinositides, edited by, S. Cockcroft, (Oxford University Press, New York, 2000), and references therein.
24. R.M. Bell and D.J. Burns, J. Biol. Chem. 266, 4661 (1991). JBCHA3 0021-9258
25. M.C. Cross and P.C. Hohenberg, Rev. Mod. Phys. 65, 851 (1993). RMPHAT 0034-6861 10.1103/RevModPhys.65.851
26. A.J. Bray and C.L. Emmott, Phys. Rev. B PRBMDO 0163-1829 52, R685 (1995). 10.1103/PhysRevB.52.R685
27. T.M. Rogers and R.C. Desai, Phys. Rev. B PRBMDO 0163-1829 39, 11956 (1989). 10.1103/PhysRevB.39.11956
28. K. John and M. Bär, Phys. Biol. PHMBA7 0031-9155 2, 123 (2005). 10.1088/1478-3975/2/2/005
29. R. Swaminathan, C.P. Hoang, and A.S. Verkmann, Biophys. J. 72, 1900 (1997). BIOJAU 0006-3495
30. O. Seksek, J. Biwersi, and A.S. Verkman, J. Cell Biol. 138, 131 (1997). JCLBA3 0021-9525 10.1083/jcb.138.1.131
31. A. Arbuzova, J. Biol. Chem. 272, 27167 (1997). JBCHA3 0021-9258 10.1074/jbc.272.43.27167
32. J. Kusba, Biophys. J. 82, 1358 (2002). BIOJAU 0006-3495