β-TrCP- and Casein Kinase II-Mediated Degradation of Cyclin F Controls Timely Mitotic Progression.

Mavrommati I., Faedda R., Galasso G., Li J., Burdova K., Fischer R., Kessler BM., Carrero ZI., Guardavaccaro D., Pagano M., D'Angiolella V.

Orderly progressions of events in the cell division cycle are necessary to ensure the replication of DNA and cell division. Checkpoint systems allow the accurate execution of each cell-cycle phase. The precise regulation of the levels of cyclin proteins is fundamental to coordinate cell division with checkpoints, avoiding genome instability. Cyclin F has important functions in regulating the cell cycle during the G2 checkpoint; however, the mechanisms underlying the regulation of cyclin F are poorly understood. Here, we observe that cyclin F is regulated by proteolysis through β-TrCP. β-TrCP recognizes cyclin F through a non-canonical degron site (TSGXXS) after its phosphorylation by casein kinase II. The degradation of cyclin F mediated by β-TrCP occurs at the G2/M transition. This event is required to promote mitotic progression and favors the activation of a transcriptional program required for mitosis.

DOI

10.1016/j.celrep.2018.08.076

Type

Journal article

Journal

Cell Rep

Publication Date

25/09/2018

Volume

24

Pages

3404 - 3412

Keywords

CKII, CRLs, F-box protein, SCF, cell cycle, cyclin F, mitosis, ubiquitin, β-TrCP, Casein Kinase II, Cyclins, HEK293 Cells, HeLa Cells, Humans, Mitosis, Proteolysis, beta-Transducin Repeat-Containing Proteins

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