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Related Experiment Videos

Microtubule structure at improved resolution.

P Meurer-Grob1, J Kasparian, R H Wade

  • 1Institut de Biologie Structurale (CEA/CNRS), 41 rue Jules Horowitz, 38027 Grenoble, France.

Biochemistry
|July 4, 2001
PubMed
Summary

Microtubule architecture is determined by lateral tubulin interactions. These conserved interactions dictate microtubule stability and assembly, regardless of protofilament number.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Microtubule architecture varies across species and cell types.
  • Stabilizing agents and GTP analogue assembly influence protofilament number.

Purpose of the Study:

  • To determine the three-dimensional structure of taxotere and GMPCPP microtubules.
  • To examine dimer packing within the microtubule wall.
  • To understand the role of lateral tubulin interactions in microtubule architecture.

Main Methods:

  • Electron cryomicroscopy and helical reconstruction to 14 Å resolution.
  • Docking tubulin crystal structure into microtubule maps.
  • Calculating simulated images from atomic resolution models.

Main Results:

  • Tubulin heterodimers align head to tail along protofilaments, with beta-tubulin capping the plus end.
  • Conserved lateral interactions between tubulin dimers are consistent across different microtubule architectures.
  • GDP-tubulin conformation, induced by stathmin-like proteins, weakens lateral contacts, potentially inhibiting assembly.

Conclusions:

  • Lateral contacts between tubulin subunits are crucial for microtubule stability, rigidity, and architecture.
  • In vivo microtubule architectures likely share surface lattice organizations with in vitro assembled microtubules.
  • Understanding these interactions provides insight into microtubule dynamics and potential drug targets.

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