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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Self-Assembly of Microtubule Tactoids
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A kinesin-13 mutant catalytically depolymerizes microtubules in ADP.

Michael Wagenbach1, Sarah Domnitz, Linda Wordeman

  • 1Deptartment of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98107, USA.

The Journal of Cell Biology
|November 13, 2008
PubMed
Summary

Kinesin-13 motors, like mitotic centromere-associated kinesin, remove tubulin from microtubules. A specific mutation reveals tubulin removal occurs at the ATP hydrolysis transition state, differing from other kinesins.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Motors

Background:

  • Kinesin-13 family motor proteins are crucial for microtubule (MT) dynamics by promoting tubulin removal.
  • Microtubule turnover is essential for various cellular processes, including cell division and intracellular transport.

Purpose of the Study:

  • To investigate the mechanism of tubulin dimer removal by kinesin-13 motors.
  • To characterize the unique conformation and catalytic cycle of a specific kinesin-13 mutant (E491A).
  • To elucidate the relationship between ATP hydrolysis and tubulin release in kinesin-13 function.

Main Methods:

  • Utilized a point mutant (E491A) of the kinesin-13 family member mitotic centromere-associated kinesin/Kif2C.
  • Studied tubulin dimer removal from stabilized microtubules in the presence of adenosine triphosphate (ATP) and adenosine diphosphate (ADP).
  • Analyzed the catalytic cycle and tubulin binding affinity of the mutant motor.

Main Results:

  • The E491A mutant isolates a distinct tubulin-removal conformation of kinesin-13.
  • Tubulin removal by the mutant is stoichiometric in ATP but catalytic only in ADP due to altered tubulin dimer release kinetics.
  • The motor regenerates catalytically in ADP, enabling further cycles of microtubule disassembly.

Conclusions:

  • Kinesin-13 mediated tubulin release from microtubules occurs at the transition state of ATP hydrolysis.
  • This mechanism represents a significant divergence in ATP turnover coupling compared to motile kinesins.
  • The findings provide new insights into the regulation and function of microtubule-severing kinesins.