Activation of cyclin B1–Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis

Abstract

A biosensor for cyclin B–Cdk1 activity shows that it uses an unconventional yet simple mechanism for nuclear accumulation.

Identification of fibroblast growth factor-8b target genes associated with early and late cell cycle events in breast cancer cells

“…Nuclear translocation of cyclin B1 has long been thought to be dependent on its phosphorylation by Plk1 (Toyoshima-Morimoto et al, 2001). Recent data suggest however that the nuclear import of cyclin B1 does not require Plk1 (Gavet and Pines, 2010). Plk1 belongs to the Polo like kinase family which in human has five identified members with roles in cell division.…”

The tumor suppressor tuberin regulates mitotic onset through the cellular localization of cyclin B1

“…15 While the mechanism of rapid import at mitosis has not been resolved, it is thought to rely on CDK1-mediated cytoplasmic and nuclear reorganization of the import machinery. 16 Once in the nucleus, modification within the nuclear export sequence (NES) of CycB1 inhibits CRM1-mediated export and supports CycB1 nuclear accumulation. 17,18 In this study, we demonstrate that tuberin binds CycB1 in a yeast two-hybrid screen.…”

Cyclin B1 interacts with the BH3-only protein Bim and mediates its phosphorylation by Cdk1 during mitosis

“…Entry into mitosis is controlled by Cdk1, which forms a bipartite complex with cyclin B and phosphorylates a spectrum of substrates that coordinate nuclear envelope breakdown, chromosome condensation, assembly of the mitotic spindle and activation of the spindle assembly checkpoint. 20 Recently a pro-apoptotic role for Cdk1 has been described, wherein it phosphorylates the anti-apoptotic Bcl-2 family members, Bcl-2, Bcl-X L and Mcl-1. [21][22][23] Phosphorylation of Bcl-2 and Bcl-X L blocks their anti-apoptotic effect, whereas phosphorylation of Mcl-1 during sustained mitotic arrest results in its Cdc20-dependent degradation and inactivation.…”