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A P53-Phosphoinositide Signalosome Regulates Nuclear AKT Activation
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Abstract
The tumour suppressor p53 and PI3K-AKT pathways have fundamental roles in the regulation of cell growth and apoptosis, and are frequently mutated in cancer. Here, we show that genotoxic stress induces nuclear AKT activation through a p53-dependent mechanism that is distinct from the canonical membrane-localized PI3K-AKT pathway. Following genotoxic stress, a nuclear PI3K binds p53 in the non-membranous nucleoplasm to generate a complex of p53 and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P 3), which recruits AKT, PDK1 and mTORC2 to activate AKT and phosphorylate FOXO proteins, thereby inhibiting DNA damage-induced apoptosis. Wild-type p53 activates nuclear AKT in an on/off fashion following stress, whereas mutant p53 dose-dependently stimulates high basal AKT activity. The p53-PtdIns(3,4,5)P 3 complex is dephosphorylated to p53-phosphatidylinositol 4,5-bisphosphate by PTEN to inhibit AKT activation. The nuclear p53-phosphoinositide signalosome is distinct from the canonical membrane-localized pathway and insensitive to PI3K inhibitors currently in the clinic, which underscores its therapeutic relevance.
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“While years of research have primarily investigated AKT signaling at the cell membrane, recent works by Chen et al. [71] and Choi et al. [61] have revealed that, under genotoxic stress, IPMK-generated nuclear PIP3 binds to p53, which activates nuclear AKT signaling and suppresses apoptosis.”
From From Obscurity to Prominence: IPMK’s Expanding Role in Cellular Signaling, Physiology, and Disease (2025) · cites this paper as [71]
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“While years of research have primarily investigated AKT signaling at the cell membrane, recent works by Chen et al. [71] and Choi et al. [61] have revealed that, under genotoxic stress, IPMK-generated nuclear PIP3 binds to p53, which activates nuclear AKT signaling and suppresses apoptosis.”
Lawal, O., Niihori, M., James, J., Hinkle, A. J., Sano, T., McClain, N., Rafikov, R., & Rafikova, O. (2025) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2024-0296oc · Cited by 1
Wang, F., Hu, L., Zeng, X., You, W., Li, H., Liu, B., & Zhang, X. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123934 · Cited by 1
Phosphoinositide dynamics in virus-associated malignancies
Li, M., Zhong, W., Hirsch, E., & Yan, D. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.09.002 · Cited by 1
FOXO4-DRI regulates endothelial cell senescence via the P53 signaling pathway
Hu, Z., Li, F., Hu, C., Shan, Q., Tang, Z., Jiang, M., Yi, X., Chen, X., Jin, L., Wang, X., et al. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2025.1729166 · Cited by 1
Zhuang, X., Lin, N., & Xu, Y. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2026.1680422 · Cited by 1
NRF2 stabilization by isoform-specific nuclear phosphoinositides in stress response
Tang, Y., Chen, Y., Carrillo, N. D., Cryns, V. L., Anderson, R. A., Sun, J., & Chen, M. (2026) · Oral Science and Homeostatic Medicine · doi:10.26599/oshm.2026.9610041 · Cited by 1
Self-citationTenkutytė, M., Kalvelytė, A. V., & Stulpinas, A. (2026) · Pharmaceuticals · doi:10.3390/ph19030509 · Cited by 1
Ying, X., Zhang, K., Jiang, S., Chen, L., Li, J.-J., Liu, G.-Y., Yu, K.-D., Wu, J., Di, G. H., Wang, Y.-Y., et al. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218503 · Cited by 1
Self-citationLipid transfer proteins and PI4KIIα generate a phosphoinositide-linked proteome
Carrillo, N. D., Chen, M., Awasthi, P., Wen, T., Chen, X., Vũ, G. T., Brahmbhatt, D., Herlihy, M., Minkoff, B. B., Sussman, M., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113089 · Cited by 1
Self-citationDong, Q., Endo, M., Kawamura, G., & Ozawa, T. (2022) · Cells · doi:10.3390/cells11193136 · Cited by 1
Beceiro, M. S. (2010) · Revista de derecho urbanístico y medio ambiente/Revista de derecho urbanístico y medio ambiente
Reconstructing emergent biological phenomena through comparative functional architectonicsPreprint
Pérez, V., & Lyubarsky, G. Y. (2023) · Qeios · doi:10.32388/uri5sf
Mo, L., Zhao, G., Li, X., He, N., Xiao, X., Xu, H.-X., & Yu, Y. (2023) · Research Square · doi:10.21203/rs.3.rs-3707525/v1
Enhanced PI3K/Akt Signaling in Response to p85α Loss is Regulated by Endosomal PI3Kα and PI3PPreprint
Thapa, N., Chen, M., Cryns, V. L., & Anderson, R. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.10.575035
Self-citation
Metadata
- Authors
- Chen, M., Choi, S., Wen, T., Chen, C., Thapa, N., Lee, J. H., Cryns, V. L., & Anderson, R. A.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Cryns, Vincent L.
- Anderson, Richard A.
- Venue
- Nature Cell Biology
- Published
- 2022-07
- Volume
- 24
- Issue
- 7
- Pages
- 1099-1113
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC9833102
- OpenAlex
- W4284709570
- Cited by
- 117
- References
- 73
- Citations by year
- 2026: 20 · 2025: 44 · 2024: 27 · 2023: 18 · 2022: 7
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Nature Cell Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Defense (W81XWH-17-1-025, W81XWH-17-1-0259)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Keywords
- p53, PI3K/Akt signaling, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 4,5-bisphosphate, PTEN, PDK1, mTORC2, genotoxic stress, DNA damage-induced apoptosis, tumour suppressor
- MeSH terms
- Cell Nucleus, Phosphatidylinositols, Tumor Suppressor Protein p53, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-akt
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