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Mechanism of Catalytic Microtubule Depolymerization via KIF2-Tubulin Transitional Conformation

Tadayuki Ogawa1, Shinya Saijo2, Nobutaka Shimizu2

  • 1Department of Cell Biology and Anatomy, University of Tokyo, Graduate School of Medicine Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Cell Reports
|September 14, 2017
PubMed

Insights

KIF2, a motor protein, depolymerizes microtubules by binding two tubulin dimers. This detailed mechanism reveals how KIF2 drives microtubule depolymerization through ATP hydrolysis.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Microtubules (MTs) are essential for cell structure and movement.
  • Microtubule-associated motors facilitate MT functions.
  • KIF2 is a unique kinesin that depolymerizes MTs during ATP hydrolysis.

Purpose of the Study:

  • To elucidate the catalytic mechanism of KIF2-driven microtubule depolymerization.
  • To understand the structural basis of KIF2's processive depolymerization activity.

Main Methods:

  • Atomic force microscopy
  • Size-exclusion chromatography
  • Multi-angle light scattering
  • Small-angle X-ray scattering
  • Analytical ultracentrifugation
  • Mass spectrometry
  • X-ray crystallography

Main Results:

  • Identified a KIF2-tubulin complex conformation where one KIF2core domain binds two tubulin dimers.
  • This 1:2 complex exists in a pre-hydrolysis state crucial for catalytic depolymerization.
  • X-ray crystallography revealed an activated KIF2core domain conformation enabling this large complex.

Conclusions:

  • The study elucidates the structural mechanism of KIF2-mediated microtubule depolymerization.
  • A 1:2 KIF2core-tubulin dimer complex is critical for KIF2's catalytic activity.
  • Understanding KIF2's mechanism provides insights into microtubule dynamics and motor protein function.
Keywords:
ATP hydrolysisKIF2MCAKcatalytic depolymerizationkinesin-13microtubulemicrotubule destabilizermolecular motor

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