Hostname: page-component-76fb5796d-2lccl Total loading time: 0 Render date: 2024-04-28T01:02:51.116Z Has data issue: false hasContentIssue false
  • English
  • Français

Reptation of Microtubules in F-Actin Networks : Effects of Filament Stiffness and Network Topology on Reptation Dynamics

Published online by Cambridge University Press:  15 February 2011

Jagesh V. Shah ,
Lisa A. Flanagan ,
David Bahk  and
Paul A. Janmey
Jagesh V. Shah
Affiliation:
Harvard-MIT Division of Health Sciences and Technology, Cambridge MA 02138, jvshah@mit.edu
Lisa A. Flanagan
Affiliation:
Div. of Experimental Medicine, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Ave., LMRC 301, Boston, MA 02115
David Bahk
Affiliation:
Div. of Experimental Medicine, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Ave., LMRC 301, Boston, MA 02115
Paul A. Janmey
Affiliation:
Div. of Experimental Medicine, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Ave., LMRC 301, Boston, MA 02115
Get access

Abstract

The thermally driven motions of fluorescently labeled microtubules embedded in a network of filamentous actin polymers are analysed as the diffusion of a rod-like polymer within a virtual tube formed by the surrounding semiflexible actin filaments. The apparent diffusion constant parallel to the tube scales with the inverse of the microtubule length and the magnitude is consistant with diffusion through a medium with a viscosity of approximately 10 centipoise. Introduction of crosslinks between the actin filaments does not alter the diffusion of the microtubules in the actin network.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 489: Symposium K – Materials Science of the Cell , 1997 , 27
Copyright
Copyright © Materials Research Society 1998

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Fuchs, E., Annu Rev Genet. 30, 197–231 (1996).Google Scholar
2. Yanagida, T., Nakase, M., Nishiyama, K., Oosawa, F., Nature. 307, 58–60 (1984).Google Scholar
3. Perkins, T.T., Smith, D.E., Chu, S., Science. 264, 819–22 (1994).Google Scholar
4. Käs, J., Strey, H., Sackmann, E., Nature. 368, 226–229 (1994).Google Scholar
5. Gittes, F., Mickey, B., Nettleton, J., Howard, J., J Cell Biol. 120, 923–34 (1993).Google Scholar
6. Riveline, D., Wiggins, C.H., Goldstein, R.E., Ott, A., Physical Review A. 56, R1330–R1333 (1997).Google Scholar
7. Spudich, J.A. and Watt, S., J Biol Chem. 246, 4866–71 (1971).Google Scholar
8. Pluta, M.. (1988) Advanced Light Microscopy. Elsevier, New York. 464.Google Scholar
9. Edwards, S.F., Proc. Phys. Soc. 92, 9–16 (1967).Google Scholar
10. Gennes, P.G. de, J Chem Phys. 55, 572–79 (1971).Google Scholar
11. Käs, J., Strey, H., Tang, J.X., Finger, D., Ezzell, R., Sackmann, E., Janmey, P.A., Biophysical Journal. 70, 609–25 (1996).Google Scholar
12. Janmey, P.A., Hvidt, S., Lamb, J., Stossel, T.P., Nature. 345, 89–92 (1990).Google Scholar