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Phospho PTEN mediated dephosphorylation of mitotic kinase PLK1 and Aurora Kinase A prevents aneuploidy and preserves genomic stability

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Abstract

PTEN, dual phosphatase tumor suppressor protein, is found to be frequently mutated in various cancers. Post-translational modification of PTEN is important for its sub-cellular localization and catalytic functions. But how these modifications affect cytological damage and aneuploidy is not studied in detail. We focus on the role of phosphatase activity along with C-terminal phosphorylation of PTEN in perspective of cytological damage like micronucleus, nuclear bud, and nuclear bridge formation. Our data suggest that wild-type PTEN, but not phospho-mutant PTEN significantly reduces cytological damage in PTEN null PC3 cells. In case of phosphatase-dead PTEN, cytological damage markers are increased during 24 h recovery after DNA damage. When we use phosphorylation and phosphatase-dead dual mutant PTEN, the extent of different cytological DNA damage parameters are similar to phosphatase-dead PTEN. We also find that both of those activities are essential for maintaining chromosome numbers. PTEN null cells exhibit significantly aberrant γ-tubulin pole formation during metaphase. Interestingly, we observed that p-PTEN localized to spindle poles along with PLK1 and Aurora Kinase A. Further depletion of phosphorylation and phosphatase activity of PTEN increases the expression of p-Aurora Kinase A (T288) and p-PLK1 (T210), compared to cells expressing wild-type PTEN. Again, wild-type PTEN but not phosphorylation-dead mutant is able to physically interact with PLK1 and Aurora Kinase A. Thus, our study suggests that the phosphorylation-dependent interaction of PTEN with PLK1 and Aurora Kinase A causes dephosphorylation of those mitotic kinases and by lowering their hyperphosphorylation status, PTEN prevents aberrant chromosome segregation in metaphase.

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Acknowledgements

This work is financially supported by The Department of Science and Technology (DST-SERB), Government of India (Sanction No. EMR/2016/001151). Ginia Ghosh was awarded a fellowship from the Council of Scientific and Industrial Research (Sanction no. 37(1673)/16/EMR-II). Prof. Dr. W.R. Sellers of Harvard Medical School generously donated hosphor-deficient PTEN and wild-type PTEN. We also appreciate and thank Dr. Prosenjit Sen of the Indian Association for Science for providing confocal microscopy.

Funding

This study is supported by the Department of Science and Technology, Republic of India, EMR/2016/001151 to Parimal Karmakar.

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  1. Department of Life Science and Biotechnology, Jadavpur University, Kolkata, West Bengal, India

    Ginia Ghosh, Rachayeeta Ray, Sougata Ghosh Chowdhury & Parimal Karmakar

  2. Department of Microbiology, Bidhannagar College, Salt Lake, Kolkata, West Bengal, India

    Sandip Misra

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Ghosh, G., Misra, S., Ray, R. et al. Phospho PTEN mediated dephosphorylation of mitotic kinase PLK1 and Aurora Kinase A prevents aneuploidy and preserves genomic stability. Med Oncol 40, 119 (2023). https://doi.org/10.1007/s12032-023-01985-z

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