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Fbw7 and Usp28 Regulate Myc Protein Stability in Response to DNA Damage

Nikita Popov, Steffi Herold, Maria Llamazares, Christina Schülein and Martin Eilers

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The cellular levels of the Myc oncoprotein are critical determinants of cell proliferation, cell growth and apoptosis and are tightly regulated by external growth factors. Levels of Myc oncoprotein also decline in response to intracellular stress signals such as DNA damage. We show here that this decline is in part due to proteasomal degradation and that it is mediated by the Fbw7 ubiquitin ligase. We have shown previously that the ubiquitin-specific protease Usp28, binds to the nucleoplasmic isoform of Fbw7, Fbw7α, and counteracts its function in mammalian cells. Usp28 dissociates from Fbw7α in response to UV irradiation, providing a mechanism how Fbw7-mediated degradation of Myc is enhanced upon DNA damage. Our data extend previous observations that link Myc function to the cellular response to DNA damage.

Authors

Nikita Popov

Institute of Molecular Biology and Tumor Research (IMT); Marburg, Germany

Steffi Herold

Institute of Molecular Biology and Tumor Research (IMT); Marburg, Germany

Maria Llamazares

Institute of Molecular Biology and Tumor Research (IMT); Marburg, Germany

Christina Schülein

Institute of Molecular Biology and Tumor Research (IMT); Marburg, Germany

Martin Eilers

Institute of Molecular Biology and Tumor Research (IMT); Marburg, Germany

Purchase article for $19

Subscribe to this journal for $129/year