Author
Listed:
- Sergio A. Rincon
(Institut Curie, PSL Research University, CNRS, UMR 144)
- Adam Lamson
(University of Colorado)
- Robert Blackwell
(University of Colorado)
- Viktoriya Syrovatkina
(University of Pennsylvania)
- Vincent Fraisier
(Institut Curie, PSL Research University, CNRS, UMR 144)
- Anne Paoletti
(Institut Curie, PSL Research University, CNRS, UMR 144)
- Meredith D. Betterton
(University of Colorado)
- Phong T. Tran
(Institut Curie, PSL Research University, CNRS, UMR 144
University of Pennsylvania)
Abstract
Bipolar spindle assembly requires a balance of forces where kinesin-5 produces outward pushing forces to antagonize the inward pulling forces from kinesin-14 or dynein. Accordingly, Kinesin-5 inactivation results in force imbalance leading to monopolar spindle and chromosome segregation failure. In fission yeast, force balance is restored when both kinesin-5 Cut7 and kinesin-14 Pkl1 are deleted, restoring spindle bipolarity. Here we show that the cut7Δpkl1Δ spindle is fully competent for chromosome segregation independently of motor activity, except for kinesin-6 Klp9, which is required for anaphase spindle elongation. We demonstrate that cut7Δpkl1Δ spindle bipolarity requires the microtubule antiparallel bundler PRC1/Ase1 to recruit CLASP/Cls1 to stabilize microtubules. Brownian dynamics-kinetic Monte Carlo simulations show that Ase1 and Cls1 activity are sufficient for initial bipolar spindle formation. We conclude that pushing forces generated by microtubule polymerization are sufficient to promote spindle pole separation and the assembly of bipolar spindle in the absence of molecular motors.
Suggested Citation
Sergio A. Rincon & Adam Lamson & Robert Blackwell & Viktoriya Syrovatkina & Vincent Fraisier & Anne Paoletti & Meredith D. Betterton & Phong T. Tran, 2017.
"Kinesin-5-independent mitotic spindle assembly requires the antiparallel microtubule crosslinker Ase1 in fission yeast,"
Nature Communications, Nature, vol. 8(1), pages 1-12, August.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15286
DOI: 10.1038/ncomms15286
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