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    Home > Biochemistry News > Biotechnology News > The deubiquitinase USP7 is a novel cyclin F interaction protein that regulates the stability of cyclin F protein

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

    • Last Update: 2023-01-05
    • Source: Internet
    • Author: User
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    Cyclin F interacts
    with USP7.

    A new research paper, published in the journal Aging, titled "Deubiquitinase USP7 is a novel cyclin F interacting protein and regulates cyclin F stability
    .
    " ”

    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, researchers Savitha S.
    Sharma, W.
    Jack Pledger and Paturu Kondaiah from the Indian Institute of Science, Sri Shankara Cancer Hospital and Research Centre and the Huntsman Cancer Institute at the University of Utah identified the deubiquitinase USP7 as a novel 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 researchers noted.

    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," the researchers said
    .


              

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