The E3 ubiquitin ligase TRIP12 participates in cell cycle progression and chromosome stability

被引：24

作者：

Larrieu, D. ^{[1
]}

Brunet, M. ^{[1
]}

Vargas, C. ^{[1
]}

Hanoun, N. ^{[1
]}

Ligat, L. ^{[1
]}

Dagnon, L. ^{[1
]}

Lulka, H. ^{[1
]}

Pommier, R. M. ^{[2
]}

Selves, J. ^{[1
]}

Jady, B. E. ^{[3
]}

Bartholin, L. ^{[2
]}

Cordelier, P. ^{[1
]}

Dufresne, M. ^{[1
]}

Torrisani, J. ^{[1
]}

机构：

[1] Univ Toulouse III Paul Sabatier, Univ Toulouse, Ctr Rech Cancerol Toulouse, INSERM, Toulouse, France

[2] Univ Lyon, Ctr Leon Berard, Ctr Rech Cancerol Lyon, Univ Claude Bernard Lyon 1,INSERM 1052,CNRS 5286, F-69008 Lyon, France

[3] Univ Toulouse III Paul Sabatier, Ctr Biol Integrat, Lab Biol Mol Eucaryote, UMR5099,CNRS, Toulouse 9, France

来源：

SCIENTIFIC REPORTS | 2020年 / 10卷 / 01期

关键词：

INTERACTING PROTEIN 12; DNA-REPLICATION; MITOSIS; COMPLEX; IDENTIFICATION; PHOSPHORYLATION; ACTIVATION; EXPRESSION; REGULATOR; DISORDER;

D O I：

10.1038/s41598-020-57762-9

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Several 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.

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页数：17

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