Protein phosphatase 2A subunit PR70 interacts with pRb and mediates its dephosphorylation
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The retinoblastoma tumor suppressor protein (pRb) regulates cell proliferation and differentiation via phosphorylation-sensitive interactions with specific targets. While the role of cyclin/cyclin-dependent kinase complexes in the modulation of pRb phosphorylation has been extensively studied, relatively little is known about the molecular mechanisms regulating phosphate removal by phosphatases. Protein phosphatase 2A (PP2A) is constituted by a core dimer bearing catalytic activity and one variable B regulatory subunit conferring target specificity and subcellular localization. We previously demonstrated that PP2A core dimer binds pRb and dephosphorylates pRb upon oxidative stress. In the present study, we identified a specific PP2A-B subunit, PR70, that was associated with pRb both in vitro and in vivo. PR70 overexpression caused pRb dephosphorylation; conversely, PR70 knockdown prevented both pRb dephosphorylation and DNA synthesis inhibition induced by oxidative stress. Moreover, we found that intracellular Ca(2+) mobilization was necessary and sufficient to trigger pRb dephosphorylation and PP2A phosphatase activity of PR70 was Ca(2+) induced. These data underline the importance of PR70-Ca(2+) interaction in the signal transduction mechanisms triggered by redox imbalance and leading to pRb dephosphorylation.
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PP2A removes phosphate from pocket proteins throughout the cell cycle; pRB is a target of PP2A/PR70, and p107, p130 and probably pRB are targets of PP2A/B55α.
“As previously mentioned, PP2A can dephosphorylate pocket proteins in all phases in cell cycle, with pRB as a target of PP2A/PR70 and p107, p130 and likely pRB as targets of PP2A/B55α (Jayadeva et al., 2010; Kurimchak et al., 2013; Magenta et al., 2008).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Magenta et al., 2008
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Magenta, A., Florio, M. C., D'Agostino, M., & Sileno, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818698-5.00001-8 · Cited by 1 · see citing works
Self-citationAlvarado, M. E., Rubiano, C. C., Sánchez, W., Díaz, A., & Wasserman, M. M. (2018) · Parasitology Research · doi:10.1007/s00436-018-6019-z
Structural Studies on PP2A and Methods in Protein Production
Magnúsdóttir, A. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Role of MicroRNAs and ZEB1 Downmodulation in Oxidative Stress-Induced Apoptosis and Senescence
Magenta, A., & Capogrossi, M. C. (2013) · Springer eBooks · doi:10.1007/978-94-007-5958-9_14
Self-citationCa2+ Controls the Epithelial Cell Quiescence-Proliferation Decision through Regulating IGF Signaling
Yi, X. (2020) · Deep Blue (University of Michigan)
- Authors
- Magenta, A., Fasanaro, P., Romani, S., Di Stefano, V., Capogrossi, M. C., & Martelli, F.
- Affiliations
- Istituto Dermopatico dell'Immacolata (IT)
- Policlinico San Donato-IRCCS, via Morandi 30, 20097, San Donato Milanese, Milan, Italy
- Corresponding author
- Martelli, Fabio
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2008-01-01
- Volume
- 28
- Issue
- 2
- Pages
- 873-882
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC2223420
- OpenAlex
- W1999624549
- Cited by
- 58
- References
- 45
- Citations by year
- 2025: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 4 · 2014: 6 · 2013: 7 · 2012: 5
- FWCI
- 1.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministero della Salute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- protein phosphatase 2A, retinoblastoma protein, pRb dephosphorylation, calcium signaling, oxidative stress, redox imbalance, protein-protein interaction, tumor suppressor regulation, DNA synthesis inhibition, PP2A regulatory subunit
- MeSH terms
- Calcium, Cells, Cultured, Humans, Hydrogen Peroxide, Mutation, Phosphorylation, Protein Binding, Retinoblastoma Protein, S Phase, Dimerization, Protein Subunits, Protein Phosphatase 2
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