Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1

@article{Neef2007ChoiceOP,
  title={Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1},
  author={R. Neef and U. Gruneberg and R. Kopajtich and Xiuling Li and E. Nigg and H. Sillj{\'e} and F. Barr},
  journal={Nature Cell Biology},
  year={2007},
  volume={9},
  pages={436-444}
}
Spatial and temporal coordination of polo-like kinase 1 (Plk1) activity is necessary for mitosis and cytokinesis, and this is achieved through binding to phosphorylated docking proteins with distinct subcellular localizations. Although cyclin-dependent kinase 1 (Cdk1) creates these phosphorylated docking sites in metaphase, a general principle that explains how Plk1 activity is controlled in anaphase after Cdk1 inactivation is lacking. Here, we show that the microtubule-associated protein… Expand
Polo-like kinase 1 regulates the stability of the mitotic centromere-associated kinesin in mitosis
Functional Dynamics of Polo-Like Kinase 1 at the Centrosome
p27Kip1 regulates the microtubule bundling activity of PRC1.
Spatial Separation of Plk1 Phosphorylation and Activity
The polo-like kinase 1 regulates CDC25B-dependent mitosis entry.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 35 REFERENCES
Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is essential for midzone formation and cytokinesis.
  • Changjun Zhu, W. Jiang
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2005
CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit.
...
1
2
3
4
...