Mps1 is SUMO-modified during the cell cycle
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Agnese Restuccia1,*, Feikun Yang2,*, Changyan Chen3, Lou Lu4, Wei Dai2
1Division of Virus-Associated Carcinogenesis, German Cancer Research Center, Heidelberg, Germany
2Departments of Environmental Medicine, Biochemistry and Molecular Pharmacology, New York University Langone Medical Center, Tuxedo Park, NY, USA
3Center for Drug Discovery, Northeastern University, Boston, MA, USA
4Division of Molecular Medicine, Department of Medicine, David Geffen School of Medicine, University of California Los Angeles, Torrance, CA, USA
*These authors contributed equally to this work
Wei Dai, e-mail: email@example.com
Keywords: Mps1, mitosis, sumoylation, BubR1
Received: August 24, 2015 Accepted: November 21, 2015 Published: December 10, 2015
Mps1 is a dual specificity protein kinase that regulates the spindle assembly checkpoint and mediates proper microtubule attachment to chromosomes during mitosis. However, the molecular mechanism that controls Mps1 protein level and its activity during the cell cycle remains unclear. Given that sumoylation plays an important role in mitotic progression, we investigated whether Mps1 was SUMO-modified and whether sumoylation affects its activity in mitosis. Our results showed that Mps1 was sumoylated in both asynchronized and mitotic cell populations. Mps1 was modified by both SUMO-1 and SUMO-2. Our further studies revealed that lysine residues including K71, K287, K367 and K471 were essential for Mps1 sumoylation. Sumoylation appeared to play a role in mediating kinetochore localization of Mps1, thus affecting normal mitotic progression. Furthermore, SUMO-resistant mutants of Mps1 interacted with BubR1 more efficiently than it did with the wild-type control. Combined, our results indicate that Mps1 is SUMO-modified that plays an essential role in regulating Mps1 functions during mitosis.
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