The Structural Basis of Force Generation by the Mitotic Motor Kinesin-5

Adeline Goulet (1) , William M Behnke-Parks (2) , Charles V Sindelar (3) , Jennifer Major (4) , Steven S Rosenfeld (4) , Carolyn A Moores (5)

1 AFMB - Architecture et fonction des macromolécules biologiques
2 Columbia University [New York]
3 YSM - Yale School of Medicine [New Haven, Connecticut]
4 Lerner Research Institute [Cleveland, OH, USA]
5 Birkbeck College [University of London]

Kinesin-5 motors are important for formation and maintenance of the bipolar mitotic spindle. Results: ATP binding triggers coupled conformational changes of kinesin-5 specific structural elements in the microtubulebound motor domain. Conclusion: Kinesin-5 mechanochemistry is tuned to its cellular functions. Significance: Subnanometer resolution structure determination of microtubule-bound kinesin-5s and kinetics experiments reveal the molecular basis of their motor properties and of drug inhibition.

Mots clés: Fluorescence; Kinesin; Kinetics; Microtubules; Mitosis; Molecular Motors; Cryoelectron Microscopy; Structural Biology

Domaines: Sciences du Vivant [q-bio]

Adeline Goulet, William M Behnke-Parks, Charles V Sindelar, Jennifer Major, Steven S Rosenfeld, et al.. The Structural Basis of Force Generation by the Mitotic Motor Kinesin-5. Journal of Biological Chemistry, 2012, 287, pp.44654 - 44666. ⟨10.1074/jbc.m112.404228⟩. ⟨hal-03573926⟩