Biochemical analyses reveal amino acid residues critical for cell cycle-dependent phosphorylation of human Cdc14A phosphatase by cyclin-dependent kinase 1
Author:
Funder
Spanish Ministry of Economy and Competitiveness
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-30253-8.pdf
Reference52 articles.
1. Bremmer, S. C. et al. Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. J Biol Chem 287, 1662–1669 (2012).
2. Kuilman, T. et al. Identification of Cdk targets that control cytokinesis. EMBO J 34, 81–96, https://doi.org/10.15252/embj.201488958 (2015).
3. Meitinger, F., Palani, S. & Pereira, G. The power of MEN in cytokinesis. Cell Cycle 11, 219–228, https://doi.org/10.4161/cc.11.2.18857 (2012).
4. Queralt, E. & Uhlmann, F. Cdk-counteracting phosphatases unlock mitotic exit. Curr Opin Cell Biol 20, 661–668 (2008).
5. Stegmeier, F. & Amon, A. Closing Mitosis: The Functions of the Cdc14 Phosphatase and Its Regulation. Annu Rev Genet (2004).
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