RETRACTED: Cancer-Associated PP2A Aα Subunits Induce Functional Haploinsufficiency and Tumorigenicity
Open accessAbstract
The introduction of SV40 small t antigen or the suppression of PP2A B56gamma subunit expression contributes to the experimental transformation of human cells. To investigate the role of cancer-associated PP2A Aalpha subunit mutants in transformation, we introduced several PP2A Aalpha mutants into immortalized but nontumorigenic human cells. These PP2A Aalpha mutants exhibited defects in binding to other PP2A subunits and impaired phosphatase activity. Although overexpression of these mutants failed to render immortalized cells tumorigenic, partial suppression of endogenous PP2A Aalpha expression activated the AKT pathway and permitted cells to form tumors in immunodeficient mice. These findings suggest that cancer-associated Aalpha mutations contribute to cancer development by inducing functional haploinsufficiency, disturbing PP2A holoenzyme composition, and altering the enzymatic activity of PP2A.
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In an in vivo knockin model of the E64G Aα mutant defective in B56α and B56δ binding, retina structure and function are not impacted.
“in an in vivo knockin model of the cancer-associated E64G Aα mutant, defective in B56α and B56δ (and potentially other B56 isoforms) binding [10,93], there was no impact on retina structure and function.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [93]
Aα E64G and E64D mutants, discovered in breast and lung carcinoma, are defective in B56α and B56δ binding in vivo and B56γ binding in vitro.
“For instance, the Aα E64G and E64D mutants, respectively discovered in breast and lung carcinoma [104], were found to be defective in B56α and B56δ binding in vivo [10], and B56γ binding in vitro [93].”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [93]
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- Authors
- Chen, W., Arroyo, J. D., Timmons, J. C., Possemato, R., & Hahn, W. C.
- Affiliations
- Brigham and Women's Hospital (US)
- Broad Institute (US)
- Venue
- Cancer Research
- Published
- 2005-09-15
- Volume
- 65
- Issue
- 18
- Pages
- 8183-8192
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2001600598
- Cited by
- 159
- References
- 50
- Citations by year
- 2025: 1 · 2024: 6 · 2023: 8 · 2022: 8 · 2021: 2 · 2020: 11 · 2019: 7 · 2018: 16 · 2017: 7 · 2016: 7 · 2015: 8 · 2014: 4 · 2013: 13 · 2012: 10
- FWCI
- 3.01
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- retraction (2024-03-15)
- Open access
- bronze
- doi.org
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (P01 CA 50661, K01CA94223, K01CA094223, P01CA050661)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- 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 Kinase Regulation and GTPase Signaling
- Keywords
- PP2A holoenzyme, tumorigenicity, cancer-associated mutations, phosphatase activity, SV40 small t antigen, AKT pathway, cell transformation, retracted article
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cell Transformation, Neoplastic, Enzyme Activation, Haploidy, Humans, Phosphoprotein Phosphatases, Mutagenesis, Site-Directed, Protein Subunits, Proto-Oncogene Proteins c-akt
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