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USP35 dimer prevents its degradation by E3 ligase CHIP through auto-deubiquitinating activity
- Title
- USP35 dimer prevents its degradation by E3 ligase CHIP through auto-deubiquitinating activity
- Authors
- Park J.; Shin S.C.; Jin K.S.; Lim M.J.; Kim Y.; Kim E.E.K.; Song E.J.
- Ewha Authors
- 송은주
- SCOPUS Author ID
- 송은주
![scopus](/images/layout/icon2.png)
- Issue Date
- 2023
- Journal Title
- Cellular and Molecular Life Sciences
- ISSN
- 1420-682X
- Citation
- Cellular and Molecular Life Sciences vol. 80, no. 4
- Keywords
- Auto-deubiquitination; CHIP; Homodimer; HSP90; USP35
- Publisher
- Springer Science and Business Media Deutschland GmbH
- Indexed
- SCIE; SCOPUS
![scopus](/images/layout/scopus2.gif)
- Document Type
- Article
- Abstract
- Recently, a number of reports on the importance of USP35 in cancer have been published. However, very little is known about the exact mechanism by which USP35 activity is regulated. Here, we show the possible regulation of USP35 activity and the structural specificity affecting its function by analyzing various fragments of USP35. Interestingly, the catalytic domain of USP35 alone does not exhibit deubiquitinating activity; in contrast, the C-terminal domain and insertion region in the catalytic domain is required for full USP35 activity. Additionally, through its C-terminal domain, USP35 forms a homodimer that prevents USP35 degradation. CHIP bound to HSP90 interacts with and ubiquitinates USP35. However, when fully functional USP35 undergoes auto-deubiquitination, which attenuates CHIP-mediated ubiquitination. Finally, USP35 dimer is required for deubiquitination of the substrate Aurora B and regulation of faithful mitotic progression. The properties of USP35 identified in this study are a unique homodimer structure, regulation of deubiquitinating activity through this, and utilization of a novel E3 ligase involved in USP35 auto-deubiquitination, which adds another complexity to the regulation of deubiquitinating enzymes. © 2023, The Author(s), under exclusive licence to Springer Nature Switzerland AG.
- DOI
- 10.1007/s00018-023-04740-9
- Appears in Collections:
- 약학대학 > 약학과 > Journal papers
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