Institut Curie, PSL Research University, Sorbonne Université CNRS, UMR 144, Paris, France
Matthieu Gélin
Institut de Recherche Saint Louis,U976 Human Immunology Pathophysiology Immunotherapy (HIPI), CytoMorpho Lab, University of Paris, INSERM, CEA, Paris, France
Liang Ji
Institut Curie, PSL Research University, Sorbonne Université CNRS, UMR 144, Paris, France
Carlos Kikuti
Institut Curie, PSL Research University, Sorbonne Université CNRS, UMR 144, Paris, France
Institut Curie, PSL Research University, Sorbonne Université CNRS, UMR 144, Paris, France
Manuel Théry
Institut de Recherche Saint Louis,U976 Human Immunology Pathophysiology Immunotherapy (HIPI), CytoMorpho Lab, University of Paris, INSERM, CEA, Paris, France; Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab, University of Grenoble-Alpes, CEA, CNRS, INRA, Grenoble, Paris, France
Institut de Recherche Saint Louis,U976 Human Immunology Pathophysiology Immunotherapy (HIPI), CytoMorpho Lab, University of Paris, INSERM, CEA, Paris, France; Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab, University of Grenoble-Alpes, CEA, CNRS, INRA, Grenoble, Paris, France
Institut Curie, PSL Research University, Sorbonne Université CNRS, UMR 144, Paris, France; Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, United States
Mitotic spindle function depends on the precise regulation of microtubule dynamics and microtubule sliding. Throughout mitosis, both processes have to be orchestrated to establish and maintain spindle stability. We show that during anaphase B spindle elongation in Schizosaccharomyces pombe, the sliding motor Klp9 (kinesin-6) also promotes microtubule growth in vivo. In vitro, Klp9 can enhance and dampen microtubule growth, depending on the tubulin concentration. This indicates that the motor is able to promote and block tubulin subunit incorporation into the microtubule lattice in order to set a well-defined microtubule growth velocity. Moreover, Klp9 recruitment to spindle microtubules is dependent on its dephosphorylation mediated by XMAP215/Dis1, a microtubule polymerase, creating a link between the regulation of spindle length and spindle elongation velocity. Collectively, we unravel the mechanism of anaphase B, from Klp9 recruitment to the motors dual-function in regulating microtubule sliding and microtubule growth, allowing an inherent coordination of both processes.
