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The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites
Open accessAbstract
We have previously shown that Greatwall kinase (Gwl) is required for M phase entry and maintenance in Xenopus egg extracts. Here, we demonstrate that Gwl plays a crucial role in a novel biochemical pathway that inactivates, specifically during M phase, “antimitotic” phosphatases directed against phosphorylations catalyzed by cyclin-dependent kinases (CDKs). A major component of this phosphatase activity is heterotrimeric PP2A containing the B55δ regulatory subunit. Gwl is activated during M phase by Cdk1/cyclin B (MPF), but once activated, Gwl promotes PP2A/B55δ inhibition with no further requirement for MPF. In the absence of Gwl, PP2A/B55δ remains active even when MPF levels are high. The removal of PP2A/B55δ corrects the inability of Gwl-depleted extracts to enter M phase. These findings support the hypothesis that M phase requires not only high levels of MPF function, but also the suppression, through a Gwl-dependent mechanism, of phosphatase(s) that would otherwise remove MPF-driven phosphorylations.
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Cites
PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
Janssens, V., Longin, S., & Goris, J. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.004 · Cited by 390
Kremmer, E., Ohst, K., Kiefer, J., Brewis, N., & Walter, G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1692 · Cited by 175
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McCloy, R. A., Rogers, S., Caldon, C. E., Lorca, T., Castro, A., & Burgess, A. (2014) · Cell Cycle · doi:10.4161/cc.28401 · Cited by 853
Targeting Mitosis in Cancer: Emerging Strategies
Dominguez-Brauer, C., Thu, K. L., Mason, J. M., Blaser, H., Bray, M. R., & Mak, T. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.11.006 · Cited by 495
Greatwall Phosphorylates an Inhibitor of Protein Phosphatase 2Α That Is Essential for Mitosis
Mochida, S., Maslen, S. L., Skehel, M., & Hunt, T. (2010) · Science · doi:10.1126/science.1195689 · Cited by 425
Self-citationA PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit
Cundell, M. J., Hutter, L. H., Nunes Bastos, R., Poser, E., Holder, J., Mohammed, S., Novak, B., & Barr, F. A. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201606033 · Cited by 193
PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93
Metadata
- Authors
- Castilho, P. V., Williams, B. C., Mochida, S., Zhao, Y., & Goldberg, M. L.
- Venue
- Molecular Biology of the Cell
- Published
- 2009-11-15
- Volume
- 20
- Issue
- 22
- Pages
- 4777-4789
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2149870815
- Cited by
- 189
- References
- 2
- FWCI
- 7.79
- Type
- journal article
- Language
- en
- Open access
- green
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- Castilho, P. V., Williams, B. C., Mochida, S., Zhao, Y., & Goldberg, M. L. (2009). The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e09-07-0643
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