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Updated: Jun 23, 2026

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
Published on: March 15, 2014
Microtubule depolymerization by the Kinesin-8 motor Kip3p: a mathematical model
L E Hough1, Anne Schwabe, Matthew A Glaser
1Physics Department, University of Colorado at Boulder, Boulder, Colorado, USA.
Abstract:
Proteins from the kinesin-8 family promote microtubule (MT) depolymerization, a process thought to be important for the control of microtubule length in living cells. In addition to this MT shortening activity, kinesin 8s are motors that show plus-end directed motility on MTs. Here we describe a simple model that incorporates directional motion and destabilization of the MT plus-end by kinesin 8. Our model quantitatively reproduces the key features of length-versus-time traces for stabilized MTs in the presence of purified kinesin 8, including length-dependent depolymerization. Comparison of model predictions with experiments suggests that kinesin 8 depolymerizes processively, i.e., one motor can remove multiple tubulin dimers from a stabilized MT. Fluctuations in MT length as a function of time are related to depolymerization processivity. We have also determined the parameter regime in which the rate of MT depolymerization is length dependent: length-dependent depolymerization occurs only when MTs are sufficiently short; this crossover is sensitive to the bulk motor concentration.
Insights
Kinesin-8 proteins shorten microtubules by moving along them. This study models kinesin-8 activity, revealing processive depolymerization and length-dependent microtubule shortening crucial for cellular control.
Area of Science:
- Cell Biology
- Molecular Motors
- Cytoskeleton Dynamics
Background:
- Kinesin-8 proteins are crucial for regulating microtubule (MT) length in cells.
- They possess both MT depolymerization activity and plus-end directed motility.
Purpose of the Study:
- To develop a simple model of kinesin-8 activity incorporating directional motion and MT plus-end destabilization.
- To quantitatively analyze kinesin-8's effect on stabilized MT length dynamics.
Main Methods:
- Development of a mathematical model for kinesin-8 motor activity.
- Quantitative comparison of model predictions with experimental data of MT length over time.
- Analysis of MT length fluctuations to infer depolymerization processivity.
Main Results:
- The model accurately reproduces experimental MT length-versus-time traces, including length-dependent depolymerization.
- Experimental data suggests kinesin-8 depolymerizes processively, removing multiple tubulin dimers per motor.
- MT length fluctuations correlate with depolymerization processivity.
Conclusions:
- Kinesin-8 exhibits processive depolymerization, contributing to microtubule length control.
- Length-dependent depolymerization occurs for shorter microtubules and is sensitive to motor concentration.
- The model provides insights into the mechanism of kinesin-8-mediated microtubule dynamics.
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