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Anchor Effect of Interactions Between Kinesin's Nucleotide-Binding Pocket and Microtubule

Yumei Jin1,2, Yizhao Geng1,2, Lina Lü1,2

  • 11Institute of Biophysics, Hebei University of Technology, Tianjin, 300401 China.

Cellular and Molecular Bioengineering
|November 14, 2019
PubMed

Insights

Microtubule binding anchors kinesin

Area of Science:

  • Molecular Biology
  • Biophysics
  • Cellular Transport

Background:

  • Microtubules serve as tracks for kinesin motors, crucial for intracellular transport.
  • Microtubule interaction modulates kinesin's mechanochemical cycle, affecting ATP hydrolysis and ADP release.
  • Kinesin's force generation involves neck linker docking, requiring microtubule-mediated head rotation.

Purpose of the Study:

  • To investigate the specific interactions between kinesin's nucleotide-binding pocket (NBP) and microtubules.
  • To elucidate the role of these interactions in kinesin's motor function and mechanochemistry.

Main Methods:

  • Utilized molecular dynamics simulations.
  • Analyzed newly obtained crystal structures of kinesin-microtubule complexes.

Main Results:

  • Identified direct interactions between kinesin's N-3 motif and negatively charged residues on α-tubulin (via Ser235 and Lys237).
  • These interactions position the NBP correctly on the microtubule, facilitating indirect binding.
  • Demonstrated the anchoring effect of these interactions on kinesin's motor domain rotation and stabilization of ATP hydrolysis.

Conclusions:

  • Specific long-range interactions between kinesin's NBP and microtubules are critical for motor function.
  • These interactions anchor kinesin's motor domain, enabling rotation and stabilizing the catalytic environment for ATP hydrolysis.
  • Ser235 acts as a key rotation center, highlighting the importance of precise molecular contacts in kinesin-microtubule dynamics.
Keywords:
Anchor effectKinesinMicrotubuleNucleotide-binding pocket

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