USP35 regulates mitotic progression by modulating the stability of Aurora B

• DOI: 10.1038/s41467-018-03107-0
• Publication Date: 2018-02-09T16:18:03Z
• Authors: Jinyoung Park; Mi-Sun Kwon; Eunice EunKyeong Kim; Hyunsook Lee; Eun Joo Song
• Keywords: Aurora B kinase; Deubiquitinating enzyme; Aurora inhibitor

Although approximately 100 deubiquitinating enzymes (DUBs) are encoded in the human genome, very little is known about DUBs that function mitosis. Here, we demonstrate DUB USP35 functions as a mitotic regulator by controlling protein levels and downstream signaling of Aurora B depletion eventually leads to several defects including cytokinesis failures. binds deubiquitinates B, inhibits APCCDH1-mediated proteasomal degradation thus maintaining its steady-state during In addition, loss decreases phosphorylation histone H3-Ser10, an substrate. Finally, transcription factor FoxM1 promotes expression USP35, well cell cycle. Our findings suggest regulates stability blocking APCCDH1-induced degradation, thereby progression.