Abstract
AbstractSeveral studies have linked the E3 ubiquitin ligase TRIP12 (Thyroid hormone Receptor Interacting Protein 12) to the cell cycle. However, the regulation and the implication of this protein during the cell cycle are largely unknown. In this study, we show that TRIP12 expression is regulated during the cell cycle, which correlates with its nuclear localization. We identify an euchromatin-binding function of TRIP12 mediated by a N-terminal intrinsically disordered region. We demonstrate the functional implication of TRIP12 in the mitotic entry by controlling the duration of DNA replication that is independent from its catalytic activity. We also show the requirement of TRIP12 in the mitotic progression and chromosome stability. Altogether, our findings show that TRIP12 is as a new chromatin-associated protein with several implications in the cell cycle progression and in the maintenance of genome integrity.
Publisher
Springer Science and Business Media LLC
Reference56 articles.
1. Chen, D., Yoon, J.-B. & Gu, W. Reactivating the ARF-p53 axis in AML cells by targeting ULF. Cell Cycle Georget. Tex 9, 2946–2951 (2010).
2. Xie, Y. & Varshavsky, A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat. Cell Biol. 4, 1003–1007 (2002).
3. Ju, D., Wang, X., Xu, H. & Xie, Y. The armadillo repeats of the Ufd4 ubiquitin ligase recognize ubiquitin-fusion proteins. FEBS Lett. 581, 265–270 (2007).
4. Keppler, B. R. & Archer, T. K. Ubiquitin-dependent and ubiquitin-independent control of subunit stoichiometry in the SWI/SNF complex. J. Biol. Chem. 285, 35665–35674 (2010).
5. Park, Y., Yoon, S. K. & Yoon, J.-B. TRIP12 functions as an E3 ubiquitin ligase of APP-BP1. Biochem. Biophys. Res. Commun. 374, 294–298 (2008).
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