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Prolonging assembly through dissociation: A self-assembly paradigm in microtubules

2009/08/31 by Sumedha, M. Leone Sumedha, Michael F. Hagan +2
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Biochemistry #Biology #Biophysics #Cell biology #Chemistry #Depolymerization #Dissociation (chemistry) #Enzyme #GTP' #Microtubule #Microtubule and mitosis dynamics #Organic chemistry #Photosynthetic Processes and Mechanisms #Plant Molecular Biology Research #Polymer chemistry #Protein filament #Tubulin #cond-mat.stat-mech #q-bio.BM #q-bio.SC

paper · pdf · doi:10.1103/physreve.83.051904

published as Phys. Rev. E 83, 051904 (2011) · accepted for publication in Physical Review E

arxiv created 2011/04/13 · openalex publication_date 2011/05/03 · arxiv updated 2015/05/13 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05

Abstract

We study a one-dimensional model of microtubule assembly and disassembly in which GTP bound to tubulins within the microtubule undergoes stochastic hydrolysis. In contrast to models that consider only a cap of GTP-bound tubulin, stochastic hydrolysis allows GTP-bound tubulin remnants to exist within the microtubule. We find that these buried GTP remnants enable an alternative mechanism of recovery from shrinkage and enhances fluctuations of filament lengths. Under conditions for which this alternative mechanism dominates, an increasing depolymerization rate leads to a decrease in dissociation rate and thus a net increase in assembly.

Citations