Sharma, SS and Pledger, WJ and Kondaiah, P (2022) The deubiquitylase USP7 is a novel cyclin F-interacting protein and regulates cyclin F protein stability. In: Aging, 14 (21). pp. 8645-8660.
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Abstract
Cyclin F, unlike canonical and transcriptional cyclins, does not bind or activate any cyclin-dependent kinases. Instead, it harbors an F-box motif and primarily functions as the substrate recognition subunit of the Skp1-Cul1-F-box E3 ubiquitin ligase complex, SCFCyclinF. By targeting specific proteins for ubiquitin-mediated proteasomal degradation, cyclin F plays a critical role in the regulation of centrosomal duplication, DNA replication and repair, and maintenance of genomic stability. Cyclin F abundance and activity are tightly regulated throughout the cell cycle. However, the molecular mechanisms regulating cyclin F are scantily understood. Here, we identify the deubiquitylase USP7 as a novel cyclin F-interacting protein. We observe that USP7 stabilizes cyclin F protein and that this function is independent of the deubiquitylase activity of USP7. Additionally, our data suggest that USP7 is also involved in the regulation of cyclin F mRNA. Pharmacological inhibition of the deubiquitylase activity of USP7 resulted in downregulation of cyclin F mRNA.
| Item Type: | Journal Article |
|---|---|
| Publication: | Aging |
| Publisher: | NLM (Medline) |
| Additional Information: | The copyright for this article belongs to the Authors. |
| Keywords: | cycline; messenger RNA; ubiquitin; ubiquitin carboxyl terminal hydrolase 7, genetics; protein stability, Cyclins; Protein Stability; RNA, Messenger; Ubiquitin; Ubiquitin-Specific Peptidase 7 |
| Department/Centre: | Division of Biological Sciences > Molecular Reproduction, Development & Genetics |
| Date Deposited: | 01 Jan 2023 07:26 |
| Last Modified: | 01 Jan 2023 07:26 |
| URI: | https://eprints.iisc.ac.in/id/eprint/78648 |
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