Protein phosphatase 2A: a target for anticancer therapy
Open accessAbstract
Protein phosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, maintains cell homoeostasis by counteracting most of the kinase-driven intracellular signalling pathways. Unrestrained activation of oncogenic kinases together with inhibition of tumour suppressors is often required for development of cancer. PP2A has been shown to be genetically altered or functionally inactivated in many solid cancers and leukaemias, and is therefore a tumour suppressor. For example, the phosphatase activity of PP2A is suppressed in chronic myeloid leukaemia and other malignancies characterised by aberrant activity of oncogenic kinases. Preclinical studies show that pharmacological restoration of PP2A tumour-suppressor activity by PP2A-activating drugs (eg, FTY720) effectively antagonises cancer development and progression. Here, we discuss PP2A as a druggable tumour suppressor in view of the possible introduction of PP2A-activating drugs into anticancer therapeutic protocols.
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PP2A complex components are mutated at a relatively low frequency in most types of human cancer.
“PP2A complex components are mutated at a relatively low frequency in most types of human cancer”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
Section 3, “PP2A in disease and cancer” (page unavailable), reports PR65β mutations in 13–15% of several primary cancers and PR65α alterations in 6.7–19.2% of several tumor categories. These figures support relatively low frequencies in the examples given, but the passage does not establish that PP2A complex components generally are mutated at low frequency in most types of human cancer; it also reports PR65α alterations in 43% of primary gliomas. (LLM, conf=0.78)
Experimental — accuracy not yet measuredCIP2A is the most prevalent oncoprotein among PP2A inhibitor proteins.
“Among them, cancerous inhibitor of PP2A (CIP2A) is the most prevalent oncoprotein”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
Section 3, “PP2A in disease and cancer” (page unavailable), says CIP2A inhibits PP2A and is overexpressed in various malignancies. It does not compare CIP2A’s prevalence with other PP2A inhibitors, so the claim that it is the most prevalent is unsupported. (LLM, conf=0.86)
Experimental — accuracy not yet measuredReactivation of PP2A is an attractive novel approach in cancer therapy.
“This establishes the reactivation of PP2A as an attractive novel approach in cancer therapy [2,6]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
PP2A inhibition promotes the various malignant characteristics of human cancer cells.
“whereas its inhibition promotes the various malignant characteristics of human cancer cells [1,2]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
Restoring PP2A activity, for example with FTY720 in leukemia, can counteract cancer, while transient PP2A inhibition, for example with LB100 in GBM, may sensitize tumors to therapy.
“Restoring PP2A activity (e.g., with FTY720 in leukemia) can counteract cancer, while transient PP2A inhibition (e.g., LB100 in GBM) may sensitize tumors to therapy [ 180 ].”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [180]
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- Authors
- Perrotti, D., & Neviani, P.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Perrotti, Danilo
- Venue
- The Lancet Oncology
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 14
- Issue
- 6
- Pages
- e229-e238
- ISSN
- 1470-2045 (ISSN-L)
- PMC
- PMC3913484
- OpenAlex
- W1987474302
- Cited by
- 400
- References
- 103
- Citations by year
- 2026: 13 · 2025: 17 · 2024: 16 · 2023: 33 · 2022: 31 · 2021: 26 · 2020: 33 · 2019: 35 · 2018: 29 · 2017: 37 · 2016: 62 · 2015: 29 · 2014: 28 · 2013: 11
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The Lancet Oncology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P50CA140158, R01CA163800, R01CA095512, P30CA016058)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- protein phosphatase 2A, tumour suppressor, cancer therapy, fingolimod, oncogenic kinase, serine/threonine phosphatase, chronic myeloid leukemia, therapeutic target
- MeSH terms
- Animals, Antineoplastic Agents, Enzyme Activation, Humans, Neoplasms, Drug Design, Signal Transduction, Enzyme Activators, Protein Phosphatase 2, Molecular Targeted Therapy
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