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Polymorphism of highly cross-linked F-actin networks: Probing multiple length scales

Lam T. Nguyen1 and Linda S. Hirst2

  • 1Department of Physics & MARTECH, Florida State University, Tallahassee, Florida 32306, USA
  • 2School of Natural Sciences, University of California, Merced, California 95344, USA

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Phys. Rev. E 83, 031910 – Published 17 March, 2011

DOI: https://doi.org/10.1103/PhysRevE.83.031910

Abstract

The assembly properties of F-actin filaments in the presence of different biological cross-linker concentrations and types have been investigated using a combined approach of fluorescence confocal microscopy and coarse-grained molecular dynamics simulation. In particular for highly cross-linked regimes, new network morphologies are observed. Complex network formation and the details of the resulting structure are strongly dependent on the ratio of cross-linkers to actin monomers and cross-linker shape but only weakly dependent on overall actin concentration and filament length. The work presented here may help to provide some fundamental understanding of how excessive cross-linkers interact with the actin filament solution, creating different structures in the cell under high cross-linker concentrations. F-actin is not only of biological importance but also, as an example of a semiflexible polymer, has attracted significant interest in its physical behavior. In combination with different cross-linkers semiflexible filaments may provide new routes to bio-materials development and act as the inspiration for new hierarchical network-based materials.

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References (41)

  1. H. Lodish, A. Berk, C. A. Kaiser, and M. Krieger, Molecular Cell Biology, 4th ed. (Freeman, New York, 1999).
  2. J. Käs, H. Strey, M. Bärmann, and M. Sackmann, Europhys. Lett. 21, 865 (1993).
  3. A. Ott, M. Magnasco, A. Simon, and A. Libchaber, Phys. Rev. E 48, 1642 (1993).
  4. J. Tang and P. Janmey, J. Biol. Chem. 271, 8556 (1996).
  5. L. Haviv, N. Gov, Y. Ideses, and A. Bernheim-Groswasser, Eur. Biophys. J. 37, 447 (2008).
  6. H. J. Kwon, A. Kakugo, K. Shikinaka, Y. Osada, and J. P. Gong, Biomacromolecules 6, 3005 (2005).
  7. M. M. A. E. Claessens, C. Semmrich, L. Ramos, and A. R. Bausch, Proc. Natl. Acad. Sci. 105, 8819 (2008).
  8. J. Bryan and R. E. Kane, J. Mol. Biol. 125, 207 (1978).
  9. J. J. Otto, R. E. Kane, and J. Bryan, Cell 17, 285 (1979).
  10. T. E. Angelini, H. Liang, W. Wriggers, and G. C. L. Wong, Proc. Natl. Acad. Sci. 100, 8634 (2003).
  11. L. T. Nguyen, W. Yang, Q. Wang, and L. S. Hirst, Soft Matter 5, 2033 (2009).
  12. R. Meyer and U. Aebi, J. Cell Biol. 110, 2013 (1990).
  13. D. H. Wachsstock, W. H. Schwarz, and T. D. Pollard, Biophys. J. 65, 205 (1993).
  14. K. A. Taylor, D. W. Taylor, and F. Schachat, J. Cell Biol. 149, 635 (2000).
  15. O. Pelletier, E. Pokidysheva, L. S. Hirst, N. Bouxsein, Y. Li, and C. R. Safinya, Phys. Rev. Lett. 91, 148102 (2003).
  16. L. S. Hirst, R. Pynn, R. Bruinsma, and C. R. Safinya, J. Chem. Phys. 123, 104902 (2005).
  17. Y. Tseng, E. Fedorov, J. M. McCaffery, S. C. Almo, and D. Wirtz, Mol. Biol. 310, 351 (2001).
  18. O. Lieleg, M. M. A. E. Claessens, C. Heussinger, E. Frey, and A. R. Bausch, Phys. Rev. Lett. 99, 088102 (2007).
  19. G. Z. Sowa, D. S. Cannell, A. J. Liu, and E. Reisler, J. Phys. Chem. B 110, 22279 (2006).
  20. M. Tempel, G. Isenberg, and E. Sackmann, Phys. Rev. E 54, 1802 (1996).
  21. M. L. Gardel, F. Nakamura, J. H. Hartwig, J. C. Crocker, T. P. Stossel, and D. A. Weitz, Proc. Natl. Acad. Sci. 103, 1762 (2006).
  22. O. Lieleg et al., Soft Matter 5, 1796 (2009).
  23. K. M. Schmoller, O. Lieleg, and A. R. Bausch, Biophys. J. 97, 83 (2009).
  24. J. H. Hartwig and T. P. Stossel, J. Mol. Biol. 145, 563 (1981).
  25. I. Borukhov, R. F. Bruinsma, W. M. Gelbart, and A. J. Liu, Proc. Natl. Acad. Sci. 102, 3673 (2005).
  26. A. Michelot et al., Curr. Biol. 16, 1924 (2006).
  27. M. Hosek and J. X. Tang, Phys. Rev. E 69, 051907 (2004).
  28. H. Fazli and R. Golestanian, Phys. Rev. E 76, 041801 (2007).
  29. P. Kraikivski, B. M. Slepchenko, and I. L. Novak, Phys. Rev. Lett. 101, 128102 (2008).
  30. O. Lieleg, M. M. A. E. Claessens, and A. R. Bausch, Soft Matter 6, 218 (2010).
  31. Y. Ideses, Y. Brill-Karniely, L. Haviv, A. Ben-Shaul, and A. Bernheim-Groswasser, PLoS ONE 3, e3297 (2008).
  32. Y. Brill-Karniely, A. B.-G. Y. Ideses, and A. Ben-Shaul, Chem. Phys. Chem. 10 (2009).
  33. H. Shin, K. R. P. Drew, J. R. Bartles, G. C. L. Wong, and G. M. Grason, Phys. Rev. Lett. 103, 238102 (2009).
  34. J. Menez et al., Oncogene 23, 2630 (2004).
  35. K. Honda et al., J. Cell Biol. 140, 1383 (1998).
  36. D. Qualtrough, K. Singh, N. Banu, C. Paraskeva, and M. Pignatelli, Br. J. Cancer 101, 1124 (2009).
  37. Y. Hashimoto et al., Clin. Cancer Res. 11, 2597 (2005).
  38. U. Gluck, D. J. Kwiatkowski, and A. Ben-Ze’ev, Proc. Natl. Acad. Sci. USA 90, 383 (2005).
  39. T. Schlick, Molecular modeling and simulation: an interdisciplinary guide (Springer-Verlag, New York, 2000).
  40. P. A. Janmey, J. Peetermans, K. S. Zaner, T. P Stossel and T. Tanaka, J. Biol. Chem. 261, 8357 (1986).
  41. J. Xu, D. Wirtz, and T. D. Pollard, J. Biol. Chem. 273, 9570 (1986).

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Phys. Rev. E 83, 031910– Published 17 March, 2011
  • Received 19 October 2010

©2011 American Physical Society

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