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Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Matthieu P M H Benoit1, Ana B Asenjo1, Hernando Sosa2
1Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
Nature Communications
|April 27, 2018
Summary
Kinesin-13 proteins depolymerize microtubules via a unique mechanism. Cryo-EM structures reveal how KLP10A induces tubulin curvature, explaining microtubule disassembly and motor protein function diversity.
Area of Science:
- Molecular Biology
- Structural Biology
- Cell Biology
Background:
- Kinesin-13s are a unique kinesin superfamily subgroup.
- They promote microtubule depolymerization but lack motility.
- The mechanism of kinesin-13 microtubule depolymerization is not fully understood.
Purpose of the Study:
- To elucidate the molecular mechanism of kinesin-13 microtubule depolymerization.
- To determine the structural basis for kinesin-13s' distinct function within the kinesin superfamily.
Main Methods:
- Near atomic resolution cryo-electron microscopy (cryo-EM).
- Structural analysis of Drosophila melanogaster kinesin-13 KLP10A constructs.
- Examination of protein bound to curved and straight tubulin in various nucleotide states.
Main Results:
- Cryo-EM structures reveal nucleotide-induced conformational changes in KLP10A.
- These changes are coupled with the movement of the kinesin-13-specific loop-2.
- This interaction induces tubulin curvature, leading to microtubule depolymerization.
Conclusions:
- Kinesin-13s utilize a distinct mechanism involving tubulin curvature induction.
- The modular structure of kinesin motor domains allows for diverse functions.
- This study provides structural insights into microtubule dynamics and motor protein adaptation.
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