USP48 Governs Cell Cycle Progression by Regulating the Protein Level of Aurora Bopen access
- Authors
- Antao, Ainsley Mike; Kaushal, Kamini; Das, Soumyadip; Singh, Vijai; Suresh, Bharathi; Kim, Kye-Seong; Ramakrishna, Suresh
- Issue Date
- Aug-2021
- Publisher
- MDPI
- Keywords
- aurora kinase; CRISPR; Cas9; DUBs; gene knockout; mitotic regulator; post-translational modifications
- Citation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.22, no.16, pp.1 - 17
- Indexed
- SCIE
SCOPUS
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Volume
- 22
- Number
- 16
- Start Page
- 1
- End Page
- 17
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/141379
- DOI
- 10.3390/ijms22168508
- ISSN
- 1661-6596
- Abstract
- Deubiquitinating enzymes play key roles in the precise modulation of Aurora B-an essential cell cycle regulator. The expression of Aurora B increases before the onset of mitosis and decreases during mitotic exit; an imbalance in these levels has a severe impact on the fate of the cell cycle. Dysregulation of Aurora B can lead to aberrant chromosomal segregation and accumulation of errors during mitosis, eventually resulting in cytokinesis failure. Thus, it is essential to identify the precise regulatory mechanisms that modulate Aurora B levels during the cell division cycle. Using a deubiquitinase knockout strategy, we identified USP48 as an important candidate that can regulate Aurora B protein levels during the normal cell cycle. Here, we report that USP48 interacts with and stabilizes the Aurora B protein. Furthermore, we showed that the deubiquitinating activity of USP48 helps to maintain the steady-state levels of Aurora B protein by regulating its half-life. Finally, USP48 knockout resulted in delayed progression of cell cycle due to accumulation of mitotic defects and ultimately cytokinesis failure, suggesting the role of USP48 in cell cycle regulation.
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