Authors
Gaven, F., Panigada, D., Portran, D., Liakopoulos, D.
Abstract
Faithful cell division requires precise control of spindle assembly and disassembly. In budding yeast, spindle breakdown at mitotic exit depends on Cdk1 inactivation and ubiquitin-mediated degradation of stabilizing factors, including the kinesin-5 Cin8 and the crosslinker Ase1/PRC1. Timely degradation of Cin8 by APCCdh1 prevents spindle over-elongation and deformation. We have identified SUMOylation and the SUMO-targeted ubiquitin ligase Slx5 as regulators of this process. Cin8 is SUMOylated and interacts with Slx5, suggesting that it is a substrate of Slx5. Deletion of the SLX5 gene or expression of a SUMOylation-defective Cin8 mutant cause spindle disassembly defects resembling those of degradation-resistant Cin8 mutants. Reduction of Cin8 SUMOylation partly stabilizes spindles in ase1{triangleup} cells. In addition, SUMOylation of Cin8 and Slx5 are required for timely Cin8 clearance from the mitotic spindle and actomyosin-ring contraction. We propose that SUMOylation regulates Cin8 activity and that SUMO-targeted ubiquitylation facilitates removal Cin8 from the spindle, promoting spindle disassembly at the end of mitosis.
Preprint server:
bioRxiv
The authors list and abstract were imported from bioRxiv on 12 Nov 2025.
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