Abstract

Microtubules play an essential role in breaking cellular symmetry. We have previously shown that separase associates with microtubules and regulates microtubule-dependent establishment of cell polarity in Arabidopsis. However, separase lacks microtubule-binding activity, raising questions about mechanisms underlying this phenomenon. Here we report that the N-terminal non-catalytic domain of separase binds to the C-terminal tail domain of three homologs of the centromeric protein CENP-E Kinesin 7 (Kin7). Conformational changes of Kin7 induced upon binding to separase facilitate recruitment of Kin7/separase complex (KISC) onto microtubules. KISC operates independently of proteolytic activity of separase in promoting microtubule rescue and pauses, as well as in suppressing catastrophes. Genetic complementation experiments in conditional separase mutant rsw4 background demonstrate the importance of KISC for the establishment of cell polarity and for plant development. Our study establishes a mechanism governing microtubule dynamics via the separase-dependent activation of CENP-E-related kinesins.

Published in

Developmental Cell
2016, Volume: 37, number: 4, pages: 350-361
Publisher: CELL PRESS

SLU Authors

• Moschou, Panagiotis Nikolaou

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    

• Gutierrez, Emilio

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    
  • The Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences
    

• Bozhkov, Peter

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    
  • The Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Cell Biology


Publication identifier

DOI: https://doi.org/10.1016/j.devcel.2016.04.015

Permanent link to this page (URI)

https://res.slu.se/id/publ/76310