The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
AMPK Promotes p53 Acetylation via Phosphorylation and Inactivation of SIRT1 in Liver Cancer Cells
Open accessAbstract
AMP-activated protein kinase (AMPK), a biologic sensor for cellular energy status, has been shown to act upstream and downstream of known tumor suppressors. However, whether AMPK itself plays a tumor suppressor role in cancer remains unclear. Here, we found that the α2 catalytic subunit isoform of AMPK is significantly downregulated in hepatocellular carcinoma (HCC). Clinicopathologic analysis revealed that underexpression of AMPK-α2 was statistically associated with an undifferentiated cellular phenotype and poor patient prognosis. Loss of AMPK-α2 in HCC cells rendered them more tumorigenic than control cells both in vitro and in vivo. Mechanistically, ectopic expression of AMPK enhanced the acetylation and stability of p53 in HCC cells. The p53 deacetylase, SIRT1, was phosphorylated and inactivated by AMPK at Thr344, promoting p53 acetylation and apoptosis of HCC cells. Taken together, our findings suggest that underexpression of AMPK is frequently observed in HCC, and that inactivation of AMPK promotes hepatocarcinogenesis by destabilizing p53 in a SIRT1-dependent manner. Cancer Res; 72(17); 4394–404. ©2012 AACR.
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Cites
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650
AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638
Self-citationDNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
LKB1 and AMP-activated protein kinase control of mTOR signalling and growth
Shaw, R. J. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01972.x · Cited by 644
AMP-activated protein kinase: Also regulated by ADP?
Hardie, D. G., Carling, D., & Gamblin, S. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.004 · Cited by 187
Self-citation
Cited by
P53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080
Michelotti, G. A., Machado, M. V., & Diehl, A. M. (2013) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2013.183 · Cited by 974
Degradation of AMPK by a Cancer-Specific Ubiquitin Ligase
Pineda, C. T., Ramanathan, S., Fon Tacer, K., Weon, J. L., Potts, M. B., Ou, Y.-H., White, M. A., & Potts, P. R. (2015) · Cell · doi:10.1016/j.cell.2015.01.034 · Cited by 389
LKB1 and AMPK and the cancer-metabolism link - ten years after
Hardie, D. G., & Alessi, D. R. (2013) · BMC Biology · doi:10.1186/1741-7007-11-36 · Cited by 301
Self-citationAMP ‐activated protein kinase: a key regulator of energy balance with many roles in human disease
Grahame Hardie, D. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12268 · Cited by 285
Metadata
- Authors
- Lee, C.-W., Wong, L. L.-Y., Tse, E. Y.-T., Liu, H.-F., Leong, V. Y.-L., Lee, J. M.-F., Hardie, D. G., Ng, I. O.-L., & Ching, Y.-P.
- Venue
- Cancer Research
- Published
- 2012-08-30
- Volume
- 72
- Issue
- 17
- Pages
- 4394-4404
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2115750021
- Cited by
- 215
- References
- 8
- FWCI
- 8.02
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Lee, C.-W., Wong, L. L.-Y., Tse, E. Y.-T., Liu, H.-F., Leong, V. Y.-L., Lee, J. M.-F., Hardie, D. G., Ng, I. O.-L., & Ching, Y.-P. (2012). AMPK Promotes p53 Acetylation via Phosphorylation and Inactivation of SIRT1 in Liver Cancer Cells. Cancer Research. https://doi.org/10.1158/0008-5472.can-12-0429
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