The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity
Open accessAbstract
SIRT1 is a NAD-dependent deacetylase that regulates a variety of pathways including the stress protection pathway. SIRT1 deacetylates a number of protein substrates, including histones, FOXOs, PGC-1alpha, and p53, leading to cellular protection. We identified a functional interaction between cJUN N-terminal kinase (JNK1) and SIRT1 by coimmunoprecipitation of endogenous proteins. The interaction between JNK1 and SIRT1 was identified under conditions of oxidative stress and required activation of JNK1 via phosphorylation. Modulation of SIRT1 activity or protein levels using nicotinamide or RNAi did not modify JNK1 activity as measured by its ability to phosphorylate cJUN. In contrast, human SIRT1 was phosphorylated by JNK1 on three sites: Ser27, Ser47, and Thr530 and this phosphorylation of SIRT1 increased its nuclear localization and enzymatic activity. Surprisingly, JNK1 phosphorylation of SIRT1 showed substrate specificity resulting in deacetylation of histone H3, but not p53. These findings identify a mechanism for regulation of SIRT1 enzymatic activity in response to oxidative stress and shed new light on its role in the stress protection pathway.
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Cites
Proceedings of the National Academy of Sciences of the United States of America
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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
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“Consistent with this concept, extra copies of sirtuin genes increase survival in model organisms, including yeast, flies, and worms [2,3,4].”
BackgroundNegative Control of p53 by Sir2α Promotes Cell Survival under Stress
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Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
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Self-citationSirtuins in mammals: insights into their biological function
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Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
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The JNK signal transduction pathway
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The Sir2 Family of Protein Deacetylases
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Sir2 mediates longevity in the fly through a pathway related to calorie restriction
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Cited by
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008
Redox regulation of SIRT1 in inflammation and cellular senescence
Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503
Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?
Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
AMP-activated protein kinase and its downstream transcriptional pathways
Cantó, C., & Auwerx, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0454-z · Cited by 421
Metadata
- Authors
- Nasrin, N., Kaushik, V. K., Fortier, E., Wall, D., Pearson, K. J., de Cabo, R., & Bordone, L.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2009-12-22
- Volume
- 4
- Issue
- 12
- Pages
- e8414
- ISSN
- 1932-6203 (ISSN-L)
- OpenAlex
- W1967901428
- Cited by
- 271
- References
- 27
- FWCI
- 13.29
- Type
- journal article
- Language
- en
- Open access
- gold
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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