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Physical Review E

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Dynamic instability of microtubules: Effect of catastrophe-suppressing drugs

Pankaj Kumar Mishra, Ambarish Kunwar, Sutapa Mukherji, and Debashish Chowdhury^*

Department of Physics, Indian Institute of Technology, Kanpur 208016, India

^*Corresponding author. Electronic address: debch@iitk.ac.in

Phys. Rev. E 72, 051914 – Published 9 November, 2005

DOI: https://doi.org/10.1103/PhysRevE.72.051914

Abstract

Microtubules are stiff filamentary proteins that constitute an important component of the cytoskeleton of cells. These are known to exhibit a dynamic instability. A steadily growing microtubule can suddenly start depolymerizing very rapidly; this phenomenon is known as a “catastrophe.” However, often a shrinking microtubule is “rescued” and starts polymerizing again. Here we develop a model for the polymerization-depolymerization dynamics of microtubules in the presence of catastrophe-suppressing drugs. Solving the dynamical equations in the steady state, we derive exact analytical expressions for the length distributions of the microtubules tipped with drug-bound tubulin subunits as well as those of the microtubules, in the growing and shrinking phases, tipped with drug-free pure tubulin subunits. We also examine the stability of the steady-state solutions.

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References (31)

B. Alberts, J. Lewis, M. Raff, K. Roberts, and J. D. Watson, Molecular Biology of the Cell (Garland, New York, 1994).
See the following special issues of journals on the cytoskeleton: Curr. Opin. Cell Biol. 8, 1 (1996); ibid. 9, 1 (1997); Nat. Cell Biol. 2, E1 (1999); Curr. Opin. Cell Biol. 12, 17 (2000); Nature (London) 422, 739 (2003).
T. Mitchison and M. Kirschner, Nature (London) 312, 232 (1984).
T. Mitchison and M. Kirschner, Nature (London) 312, 237 (1984).
H. P. Erickson and E. T. O’Brien, Annu. Rev. Biophys. Biomol. Struct. 21, 145 (1992).
A. Desai and T. J. Mitchison, Annu. Rev. Cell Dev. Biol. 13, 83 (1997).
E. Nogales, Annu. Rev. Biophys. Biomol. Struct. 30, 397 (2001).
J. Howard and A. A. Hyman, Nature (London) 422, 753 (2003).
T. L. Hill, Proc. Natl. Acad. Sci. U.S.A. 81, 6728 (1984).
R. J. Rubin, Proc. Natl. Acad. Sci. U.S.A. 85, 446 (1988).
M. Dogterom and S. Leibler, Phys. Rev. Lett. 70, 1347 (1993).
M. Dogterom and B. Yurke, Phys. Rev. Lett. 81, 485 (1998).
H. Flyvbjerg, T. E. Holy, and S. Leibler, Phys. Rev. Lett. 73, 2372 (1994).
H. Flyvbjerg, T. E. Holy, and S. Leibler, Phys. Rev. E 54, 5538 (1996).
H. Flyvbjerg and E. Jobs, Phys. Rev. E 56, 7083 (1997).
E. Jobs, D. E. Wolf, and H. Flyvbjerg, Phys. Rev. Lett. 79, 519 (1997).
B. Houchmandzadeh and M. Vallade, Phys. Rev. E 53, 6320 (1996).
D. J. Bicout, Phys. Rev. E 56, 6656 (1997).
D. J. Bicout and R. J. Rubin, Phys. Rev. E 59, 913 (1999).
K. F. Freed, Phys. Rev. E 66, 061916 (2002).
M. Hammele and W. Zimmermann, Phys. Rev. E 67, 021903 (2003).
B. Perez-Ramirez, J. M. Andreu, M. J. Gorbunoff, and S. N. Timasheff, Biochemistry 35, 3277 (1996).
A. Vandecandelaere, S. R. Martin, M. J. Schilstra, and P. M. Bayley, Biochemistry 33, 2792 (1994).
A. Vandecandelaere, S. R. Martin, and Y. Engelbroghs, Biochem. J. 323, 189 (1997).
J. R. Peterson and T. J. Mitchison, Chem. Biol. 9, 1275 (2002).
M. A. Jordan and L. Wilson, Nat. Rev. Cancer 4, 253 (2004).
J. J. Correia and S. Lobert, Curr. Pharma. Design 7, 1213 (2001).
B. S. Govindan and W. B. Spillman, Jr., Phys. Rev. E 70, 032901 (2004).
R. A. Walker, E. T. O’Brien, N. K. Pryer, M. F. Soboiero, and W. A. Voter, J. Cell Biol. 107, 1437 (1988).
There are some errors in the formulas in Ref. [20]; here we give the corresponding corrected expressions.
D. Panda, M. A. Jordan, K. C. Chu, and L. Wilson, J. Biol. Chem. 271, 29807 (1996).