Recurrent PPP2R1A Mutations in Uterine Cancer Act through a Dominant-Negative Mechanism to Promote Malignant Cell Growth
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Abstract
Somatic missense mutations in the Ser/Thr protein phosphatase 2A (PP2A) Aα scaffold subunit gene PPP2R1A are among the few genomic alterations that occur frequently in serous endometrial carcinoma (EC) and carcinosarcoma, two clinically aggressive subtypes of uterine cancer with few therapeutic options. Previous studies reported that cancer-associated Aα mutants exhibit defects in binding to other PP2A subunits and contribute to cancer development by a mechanism of haploinsufficiency. Here we report on the functional significance of the most recurrent PPP2R1A mutations in human EC, which cluster in Aα HEAT repeats 5 and 7. Beyond predicted loss-of-function effects on the formation of a subset of PP2A holoenzymes, we discovered that Aα mutants behave in a dominant-negative manner due to gain-of-function interactions with the PP2A inhibitor TIPRL1. Dominant-negative Aα mutants retain binding to specific subunits of the B56/B′ family and form substrate trapping complexes with impaired phosphatase activity via increased recruitment of TIPRL1. Accordingly, overexpression of the Aα mutants in EC cells harboring wild-type PPP2R1A increased anchorage-independent growth and tumor formation, and triggered hyperphosphorylation of oncogenic PP2A-B56/B′ substrates in the GSK3β, Akt, and mTOR/p70S6K signaling pathways. TIPRL1 silencing restored GSK3β phosphorylation and rescued the EC cell growth advantage. Our results reveal how PPP2R1A mutations affect PP2A function and oncogenic signaling, illuminating the genetic basis for serous EC development and its potential control by rationally targeted therapies. Cancer Res; 76(19); 5719–31. ©2016 AACR.
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Mutations at P179, R183, S256, and R258, which recur in disease, markedly alter PP2A holoenzyme composition in cells.
“Interestingly, recurrent mutation of these residues (for example, P179, R183, S256, and R258) result in marked changes in the PP2A holoenzyme composition in cells (Haesen et al., 2016; O’Connor et al., 2019; Ruediger et al., 2011; Taylor et al., 2019).”
From Selective PP2A enhancement through biased heterotrimer stabilization (2020) · cites this paper as Haesen et al., 2016
Experimental — accuracy not yet measuredMost cancer-associated PPP2R1A mutations encode inactive PP2A/Aα or PP2A/Aβ scaffolds that prevent proper holoenzyme formation and promote carcinogenesis.
“Most cancer-associated mutations encode inactive PP2A/Aα or PP2A/Aβ scaffolds, which prevent proper PP2A holoenzyme formation and promote carcinogenesis (Haesen et al., 2016).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Haesen et al., 2016
GSK3β is an established substrate of the PP2A holoenzyme containing B56δ.
“GSK3 b is an established substrate of the PP2A holoenzyme containing B56 d (Lambrecht et al., 2018; Haesen et al., 2016).”
From Combination of Hypoglycemia and Metformin Impairs Tumor Metabolic Plasticity and Growth by Modulating the PP2A-GSK3β-MCL-1 Axis (2019) · cites this paper as Haesen et al., 2016
The B56δ-containing PP2A complex plays important tumor suppressor roles through its established function in the regulation of GSK3β dephosphorylation.
“Particularly, the B56 d -containing PP2A complex plays important tumor suppressor roles through its established function in the regulation of GSK3 b dephosphorylation (Lambrecht et al., 2018; Haesen et al., 2016) and possibly other substrates.”
From Combination of Hypoglycemia and Metformin Impairs Tumor Metabolic Plasticity and Growth by Modulating the PP2A-GSK3β-MCL-1 Axis (2019) · cites this paper as Haesen et al., 2016
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Self-citation
- Authors
- Haesen, D., Abbasi Asbagh, L., Derua, R., Hubert, A., Schrauwen, S., Hoorne, Y., Amant, F., Waelkens, E., Sablina, A., & Janssens, V.
- Affiliations
- KU Leuven (BE)
- 2VIB Center for the Biology of Disease, Department of Human Genetics, KU Leuven, Leuven, Belgium.
- Corresponding author
- Janssens, Veerle
- Venue
- Cancer Research
- Published
- 2016-10-01
- Volume
- 76
- Issue
- 19
- Pages
- 5719-5731
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2503721758
- Cited by
- 124
- References
- 56
- Citations by year
- 2026: 9 · 2025: 23 · 2024: 8 · 2023: 13 · 2022: 18 · 2021: 10 · 2020: 8 · 2019: 13 · 2018: 15 · 2017: 7
- FWCI
- 6.06
- Type
- journal article
- Language
- en
- Open access
- green
- lirias.kuleuven.be
- Licence
- other-oa
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Lirias (KU Leuven) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Pure Amsterdam UMC (submittedVersion)
- Funders
- Australian Government
- KU Leuven (P7/13)
- Vlaamse regering
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- 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
- Keywords
- PPP2R1A, serous endometrial carcinoma, uterine cancer, carcinosarcoma, protein phosphatase 2A, dominant negative mutation, GSK3β phosphorylation, Akt signaling, mTOR/p70S6K signaling, HEAT repeats, anchorage-independent growth, tumor formation, targeted therapy
- MeSH terms
- Animals, Female, Humans, Endometrial Neoplasms, Cystadenocarcinoma, Serous, Mutation, Missense, Ribosomal Protein S6 Kinases, 70-kDa, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Cell Proliferation, Mice, Protein Phosphatase 2, TOR Serine-Threonine Kinases
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