Activation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth
Open accessAbstract
Targeted cancer therapies, which act on specific cancer-associated molecular targets, are predominantly inhibitors of oncogenic kinases. While these drugs have achieved some clinical success, the inactivation of kinase signaling via stimulation of endogenous phosphatases has received minimal attention as an alternative targeted approach. Here, we have demonstrated that activation of the tumor suppressor protein phosphatase 2A (PP2A), a negative regulator of multiple oncogenic signaling proteins, is a promising therapeutic approach for the treatment of cancers. Our group previously developed a series of orally bioavailable small molecule activators of PP2A, termed SMAPs. We now report that SMAP treatment inhibited the growth of KRAS-mutant lung cancers in mouse xenografts and transgenic models. Mechanistically, we found that SMAPs act by binding to the PP2A Aα scaffold subunit to drive conformational changes in PP2A. These results show that PP2A can be activated in cancer cells to inhibit proliferation. Our strategy of reactivating endogenous PP2A may be applicable to the treatment of other diseases and represents an advancement toward the development of small molecule activators of tumor suppressor proteins.
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SMAPs, small molecule PP2A activators derived from phenothiazines, cause dephosphorylation of chosen pathogenic targets like c-MYC and ERK and inhibit tumors in various in vivo cancer models.
“A series of small molecule PP2A activators, previously termed SMAPs and engineered from phenothiazine parent compounds, drive dephosphorylation of select pathogenic substrates such as c-MYC and ERK with concordant tumor inhibition in an array of in vivo cancer models (Allen-Petersen et al., 2018; Kauko et al., 2018; Sangodkar et al., 2017b).”
From Selective PP2A enhancement through biased heterotrimer stabilization (2020) · cites this paper as Sangodkar et al., 2017b
The Discussion describes SMAPs as phenothiazine-derived PP2A activators, and the Results report reduced phosphorylated ERK and tumor growth in several in vivo models of KRAS-mutant lung cancer. Our copy does not report SMAP-induced dephosphorylation of c-MYC or demonstrate tumor inhibition across different cancer types. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIn standard culture, these derivatives caused no apoptosis, and in low serum their effect was much weaker by GI50.
“In line with the inability to stabilize AB56αC heterotrimers, these derivative compounds did not induce apoptosis in standard cell culture conditions and had a significantly reduced effect in low serum culture conditions as determined by GI50s (Fig. 4C; Fig S4A) (Kauko et al., 2018; McClinch et al., 2018; Sangodkar et al., 2017a; Tohmé et al., 2019).”
From Selective PP2A enhancement through biased heterotrimer stabilization (2020) · cites this paper as Sangodkar et al., 2017a
The Results report that the SMAPs tested in this paper induced cell death in cultured lung cancer cells; they do not identify those SMAPs as the derivative compounds in the citing sentence. The PP2A assay methods call TRC-766 inactive, but provide no apoptosis or low-serum GI50 result for it. Searches for derivative-compound apoptosis and low-serum GI50 comparisons found no passage addressing the attributed claim (page numbers unavailable). (LLM, conf=0.72)
Experimental — accuracy not yet measuredOrally bioavailable small-molecule activators of PP2A inhibit the growth of KRAS-mutant lung cancers in mouse xenografts and transgenic models.
“Orally bioavailable small-molecule activators of PP2A have been shown to inhibit the growth of KRAS-mutant lung cancers in mouse xenografts and transgenic models (Sangodkar et al., 2017).”
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 Sangodkar et al., 2017
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- Sangodkar J, Farrington CC, McClinch K, Galsky MD, Kastrinsky DB, Narla G. All roads lead to PP2A: exploiting the therapeutic potential of this phosphatase. FEBS J. 2016;283(6):1004-1024.
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Self-citationRABL6A inhibits tumor-suppressive PP2A/AKT signaling to drive pancreatic neuroendocrine tumor growth
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The XFP (17-BM) beamline for X-ray footprinting at NSLS-II
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- Authors
- Sangodkar, J., Perl, A., Tohme, R., Kiselar, J., Kastrinsky, D. B., Zaware, N., Izadmehr, S., Mazhar, S., Wiredja, D. D., O’Connor, C. M., Hoon, D., Dhawan, N. S., Schlatzer, D., Yao, S., Leonard, D., Borczuk, A. C., Gokulrangan, G., Wang, L., Svenson, E., Farrington, C. C., Yuan, E., Avelar, R. A., Stachnik, A., Smith, B., Gidwani, V., Giannini, H. M., McQuaid, D., McClinch, K., Wang, Z., Levine, A. C., Sears, R. C., Chen, E. Y., Duan, Q., Datt, M., Haider, S., Ma’ayan, A., DiFeo, A., Sharma, N., Galsky, M. D., Brautigan, D. L., Ioannou, Y. A., Xu, W., Chance, M. R., Ohlmeyer, M., & Narla, G.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Case Western Reserve University (US)
- Weill Cornell Medicine (US)
- University of Virginia (US)
- University of Washington (US)
- Oregon Health & Science University (US)
- International Centre for Genetic Engineering and Biotechnology (IN)
- Corresponding author
- Narla, Goutham
- ORCID
- Perl, Abbey
- Kiselar, Janna
- Zaware, Nilesh
- Izadmehr, Sudeh
- Mazhar, Sahar
- Wiredja, Danica D.
- O’Connor, Caitlin M.
- Schlatzer, Daniela
- Yao, Shen
- Borczuk, Alain C.
- Wang, Lifu
- Farrington, Caroline C.
- Avelar, Rita A.
- Smith, Blake
- Giannini, Heather M.
- McQuaid, Daniel
- Wang, Zhizhi
- Levine, Alice C.
- Sears, Rosalie C.
- Datt, Manish
- Haider, Shozeb
- Ma’ayan, Avi
- DiFeo, Analisa
- Galsky, Matthew D.
- Brautigan, David L.
- Ioannou, Yiannis A.
- Xu, Wenqing
- Chance, Mark R.
- Ohlmeyer, Michael
- Narla, Goutham
- Venue
- Journal of Clinical Investigation
- Published
- 2017-05-15
- Volume
- 127
- Issue
- 6
- Pages
- 2081-2090
- ISSN
- 0021-9738 (ISSN-L)
- 1558-8238
- PMC
- PMC5451217
- OpenAlex
- W2613638456
- Cited by
- 196
- References
- 48
- Citations by year
- 2026: 14 · 2025: 10 · 2024: 13 · 2023: 26 · 2022: 22 · 2021: 24 · 2020: 25 · 2019: 33 · 2018: 21 · 2017: 8
- FWCI
- 9.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- National Science Foundation (1228549)
- Case Western Reserve University
- National Institutes of Health (TL1TR002549)
- National Heart, Lung, and Blood Institute (U54HL127624)
- National Cancer Institute (R01CA181654, U54CA189201, F31CA213554, R01CA196228)
- National Institute of General Medical Sciences (T32GM007250)
- National Institute of Biomedical Imaging and Bioengineering (P30EB009998)
- National Center for Advancing Translational Sciences
- 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, KRAS mutation, lung cancer, SMAP, protein conformational change, targeted cancer therapy, cell proliferation inhibition
- MeSH terms
- Animals, Antineoplastic Agents, Cell Survival, Enzyme Activation, Humans, Male, Mice, Inbred BALB C, Mice, Nude, Mice, Transgenic, Protein Binding, Signal Transduction, Proto-Oncogene Proteins p21(ras), Drug Resistance, Neoplasm, Enzyme Activators, Xenograft Model Antitumor Assays, Cell Line, Tumor, Tumor Burden, Protein Phosphatase 2
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