The basic biology of PP2A in hematologic cells and malignancies
Open accessAbstract
Reversible protein phosphorylation plays a crucial role in regulating cell signaling. In normal cells, phosphoregulation is tightly controlled by a network of protein kinases counterbalanced by several protein phosphatases. Deregulation of this delicate balance is widely recognized as a central mechanism by which cells escape external and internal self-limiting signals, eventually resulting in malignant transformation. A large fraction of hematologic malignancies is characterized by constitutive or unrestrained activation of oncogenic kinases. This is in part achieved by activating mutations, chromosomal rearrangements, or constitutive activation of upstream kinase regulators, in part by inactivation of their anti-oncogenic phosphatase counterparts. Protein phosphatase 2A (PP2A) represents a large family of cellular serine/threonine phosphatases with suspected tumor suppressive functions. In this review, we highlight our current knowledge about the complex structure and biology of these phosphatases in hematologic cells, thereby providing the rationale behind their diverse signaling functions. Eventually, this basic knowledge is a key to truly understand the tumor suppressive role of PP2A in leukemogenesis and to allow further rational development of therapeutic strategies targeting PP2A.
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In mammals, the C and A subunits are each encoded by two genes, producing α and β isoforms.
“In mammals, both subunits are each encoded by two distinct genes, leading to an α and β protein isoform.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [7]
PP2A is a family of Ser/Thr phosphatases made of a catalytic C subunit and a structural A subunit, usually bound to a regulatory B-type subunit.
“Protein Phosphatase 2A (PP2A) encompasses a large family of Ser/Thr phosphatases, consisting of a catalytic C subunit and a structural A subunit that are, in most cases, further bound to a regulatory B-type subunit.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [7]
PP2A exhibits a context-dependent duality in cancer biology, functioning as both a tumor suppressor through phosphatase-mediated inactivation of growth-promoting kinases and MYC-driven transcription and as a potential tumor promoter when its regulatory subunits are hijacked to stabilize survival pathways or when specific holoenzyme complexes enhance oncogenic signaling networks.
“PP2A exhibits a context-dependent duality in cancer biology, functioning as both a tumor suppressor through its phosphatase-mediated inactivation of growth-promoting kinases (e.g., PI3K/AKT and MAPK/ERK) and MYC-driven transcription and as a potential tumor promoter when its regulatory subunits are hijacked to stabilize survival pathways or when specific holoenzyme complexes paradoxically enhance”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [178]
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References 153 · Cited by 73
- Authors
- Haesen, D., Sents, W., Lemaire, K., Hoorne, Y., & Janssens, V.
- Affiliations
- KU Leuven (BE)
- Corresponding author
- Janssens, Veerle
- Venue
- Frontiers in Oncology
- Publisher
- Frontiers Media SA
- Published
- 2014-12-11
- Volume
- 4
- Pages
- 347-347
- ISSN
- 2234-943X (ISSN-L)
- PMC
- PMC4263090
- OpenAlex
- W1974894246
- Cited by
- 73
- References
- 153
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 4 · 2020: 8 · 2019: 5 · 2018: 9 · 2017: 9 · 2016: 12 · 2015: 2
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Oncology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Lirias (KU Leuven) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Australian Government
- KU Leuven (P7/13)
- Vlaamse Liga Tegen Kanker
- Vlaamse regering
- 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 › Signaling Pathways in Disease
- Keywords
- protein phosphatase 2A, hematologic malignancies, leukemogenesis, tumor suppression, protein phosphorylation, protein kinases, PP2A inhibitors, malignant transformation
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