Dual Regulation of Fbw7 Function and Oncogenic Transformation by Usp28
نویسندگان
چکیده
منابع مشابه
Fbw7 and Usp28 – enemies and allies
The Usp28 deubiquitinase antagonizes Fbw7-mediated turnover of multiple oncoproteins, including Myc, Jun, and Notch, and promotes tumorigenesis in the intestine. Our recent study reveals that Usp28 also counteracts autocatalytic ubiquitination of Fbw7, suggesting a complex role for Usp28 in the regulation of Fbw7 activity and tumor development.
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15 صفحه اولNegative regulation of the stability and tumor suppressor function of Fbw7 by the Pin1 prolyl isomerase.
Fbw7 is the substrate recognition component of the Skp1-Cullin-F-box (SCF)-type E3 ligase complex and a well-characterized tumor suppressor that targets numerous oncoproteins for destruction. Genomic deletion or mutation of FBW7 has been frequently found in various types of human cancers; however, little is known about the upstream signaling pathway(s) governing Fbw7 stability and cellular func...
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USP28 (ubiquitin-specific protease 28) is a deubiquitinating enzyme that has been implicated in the DNA damage response, the regulation of Myc signaling, and cancer progression. The half-life stability of major regulators of critical cellular pathways depends on the activities of specific ubiquitin E3 ligases that target them for proteosomal degradation and deubiquitinating enzymes that promote...
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ژورنال
عنوان ژورنال: Cell Reports
سال: 2014
ISSN: 2211-1247
DOI: 10.1016/j.celrep.2014.09.057