MASTL overexpression promotes chromosome instability and metastasis in breast cancer
Open accessAbstract
MASTL kinase is essential for correct progression through mitosis, with loss of MASTL causing chromosome segregation errors, mitotic collapse and failure of cytokinesis. However, in cancer MASTL is most commonly amplified and overexpressed. This correlates with increased chromosome instability in breast cancer and poor patient survival in breast, ovarian and lung cancer. Global phosphoproteomic analysis of immortalised breast MCF10A cells engineered to overexpressed MASTL revealed disruption to desmosomes, actin cytoskeleton, PI3K/AKT/mTOR and p38 stress kinase signalling pathways. Notably, these pathways were also disrupted in patient samples that overexpress MASTL. In MCF10A cells, these alterations corresponded with a loss of contact inhibition and partial epithelial-mesenchymal transition, which disrupted migration and allowed cells to proliferate uncontrollably in 3D culture. Furthermore, MASTL overexpression increased aberrant mitotic divisions resulting in increased micronuclei formation. Mathematical modelling indicated that this delay was due to continued inhibition of PP2A-B55, which delayed timely mitotic exit. This corresponded with an increase in DNA damage and delayed transit through interphase. There were no significant alterations to replication kinetics upon MASTL overexpression, however, inhibition of p38 kinase rescued the interphase delay, suggesting the delay was a G2 DNA damage checkpoint response. Importantly, knockdown of MASTL, reduced cell proliferation, prevented invasion and metastasis of MDA-MB-231 breast cancer cells both in vitro and in vivo, indicating the potential of future therapies that target MASTL. Taken together, these results suggest that MASTL overexpression contributes to chromosome instability and metastasis, thereby decreasing breast cancer patient survival.
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Greatwall kinase inhibits PP2A/B55 by phosphorylating Arpp19 and/or ENSA, and its upregulation promotes tumorigenesis.
“As mentioned earlier, the main function of the Greatwall kinase (known as MASTL in mammals) is to inhibit PP2A/B55 by phosphorylating Arpp19 and/or ENSA, which are inhibitors of PP2A/B55 (reviewed in Castro and Lorca, 2018). Growing evidence suggests that upregulation of Greatwall promotes tumorigenesis (Rogers et al., 2018; Sun et al., 2017; Uppada et al., 2018).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Rogers et al., 2018
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SILAC kinase screen identifies potential MASTL substrates
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IL-22 regulates MASTL expression in intestinal epithelial cells
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- Authors
- Rogers, S., McCloy, R. A., Parker, B. L., Gallego-Ortega, D., Law, A. M. K., Chin, V. T., Conway, J. R. W., Fey, D., Millar, E. K. A., O’Toole, S., Deng, N., Swarbrick, A., Chastain, P. D., Cesare, A. J., Timpson, P., Caldon, C. E., Croucher, D. R., James, D. E., Watkins, D. N., & Burgess, A.
- Affiliations
- The University of Sydney (AU)
- Garvan Institute of Medical Research (AU)
- University College Dublin (IE)
- UNSW Sydney (AU)
- University of Illinois Chicago, Rockford campus (US)
- Corresponding author
- Burgess, Andrew
- ORCID
- Rogers, Samuel
- McCloy, Rachael A.
- Parker, Benjamin L.
- Gallego-Ortega, David
- Law, Andrew M. K.
- Chin, Venessa T.
- Conway, James R. W.
- Fey, Dirk
- Millar, Ewan K. A.
- Deng, Niantao
- Swarbrick, Alexander
- Chastain, Paul D.
- Cesare, Anthony J.
- Timpson, Paul
- Caldon, C. Elizabeth
- Croucher, David R.
- James, David E.
- Watkins, D. Neil
- Burgess, Andrew
- Venue
- Oncogene
- Published
- 2018-05-10
- Volume
- 37
- Issue
- 33
- Pages
- 4518-4533
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC6095835
- OpenAlex
- W2801550495
- Cited by
- 67
- References
- 47
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 5 · 2023: 10 · 2022: 8 · 2021: 8 · 2020: 13 · 2019: 8 · 2018: 2 · 2017: 1
- FWCI
- 4.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Oncogene (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Funders
- National Breast Cancer Foundation (IIRS-18-103)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- MASTL, breast cancer, chromosomal instability, metastasis, mitosis, PP2A-B55, p38 MAPK, PI3K/AKT/mTOR signalling, epithelial-mesenchymal transition, micronuclei, G2 DNA damage checkpoint, desmosomes, actin cytoskeleton, phosphoproteomics, MCF10A cells, MDA-MB-231 cells, cell invasion, therapeutic target
- MeSH terms
- Animals, Breast Neoplasms, DNA Damage, Female, Humans, Actin Cytoskeleton, Microtubule-Associated Proteins, Signal Transduction, Mice, SCID, Mice, Inbred NOD, Protein Serine-Threonine Kinases, Phosphatidylinositol 3-Kinases, MAP Kinase Signaling System, Chromosomal Instability, Cell Line, Tumor, Cell Proliferation, Proto-Oncogene Proteins c-akt, Mice, TOR Serine-Threonine Kinases, Epithelial-Mesenchymal Transition, Cell Cycle Checkpoints
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