The deubiquitinase USP7 is a novel cyclin F interaction protein that regulates the stability of cyclin F

"This study highlights the potential role of the cyclin F-USP7 axis in pathological conditions, including cancer and neurodegenerative diseases
.
"

The ordered progression of the cell cycle is driven
by periodic oscillations of cyclin-dependent kinase (CDKs) activity.
Cyclin F, unlike standard and transcribed cyclins, does not bind to or activate any cyclin-dependent kinases
.
Instead, it contains an F-box motif, primarily as a substrate recognition subunit
for the Skp1-Cul1-F-box E3 ubiquitin ligase complex SCFCyclin F.

By targeting specific proteins for ubiquitin-mediated proteasome degradation, cyclin F plays a key role
in regulating centrosome replication, DNA replication and repair, and maintaining genomic stability.
The abundance and activity of cyclin F are strictly regulated
throughout the cell cycle.
However, the molecular mechanism that regulates cyclin F is unclear
.

In the new study, the researchers discovered that the deubiquitinase USP7 is a new cyclin f-interacting protein
.

"In this study, we identified USP7 as a novel cyclin F interaction protein and revealed a new aspect
of cyclin F regulation mediated by this interaction.
"

The team observed that USP7 stabilizes cyclin F, and that this function is independent
of USP7's deubiquitinase activity.
In addition, their data suggest that USP7 is also involved in regulating cyclin F mRNA
.
Drug inhibition of USP7 deubiquitinase activity leads to cyclin F mRNA downregulation
.

"In conclusion, in this study, we demonstrate a new interacting partner of cyclin F, USP7, and the role of
USP7 in cyclin F mRNA and protein regulation.
" This study highlights the potential role of the cyclin F-USP7 axis in pathological conditions, including cancer and neurodegenerative diseases
.
”

DOI: https://doi.
org/10.
18632/aging.
204372