Nature Communications (May 2017)
Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
- Hyeog Kang,
- Shinichi Oka,
- Duck-Yeon Lee,
- Junhong Park,
- Angel M. Aponte,
- Young-Sang Jung,
- Jacob Bitterman,
- Peiyong Zhai,
- Yi He,
- Hamed Kooshapur,
- Rodolfo Ghirlando,
- Nico Tjandra,
- Sean B. Lee,
- Myung K. Kim,
- Junichi Sadoshima,
- Jay H. Chung
Affiliations
- Hyeog Kang
- Laboratory of Obesity and Aging Research, Genetics and Development Biology Center, National Heart Lung and Blood Institute, National Institutes of Health
- Shinichi Oka
- Department of Cell Biology and Molecular Medicine, Cardiovascular Research Institute, Rutgers University, New Jersey Medical School
- Duck-Yeon Lee
- Biochemistry Core Facility, Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute, National Institutes of Health
- Junhong Park
- Department of Pathology, Tulane University School of Medicine
- Angel M. Aponte
- Proteomics Core Facility, National Heart Lung and Blood Institute, National Institutes of Health
- Young-Sang Jung
- Integrated Metabolomics Research Group, Western Seoul Center, Korea Basic Science Institute
- Jacob Bitterman
- Laboratory of Obesity and Aging Research, Genetics and Development Biology Center, National Heart Lung and Blood Institute, National Institutes of Health
- Peiyong Zhai
- Department of Cell Biology and Molecular Medicine, Cardiovascular Research Institute, Rutgers University, New Jersey Medical School
- Yi He
- Laboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health
- Hamed Kooshapur
- Laboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health
- Rodolfo Ghirlando
- Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
- Nico Tjandra
- Laboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health
- Sean B. Lee
- Department of Pathology, Tulane University School of Medicine
- Myung K. Kim
- Laboratory of Obesity and Aging Research, Genetics and Development Biology Center, National Heart Lung and Blood Institute, National Institutes of Health
- Junichi Sadoshima
- Department of Cell Biology and Molecular Medicine, Cardiovascular Research Institute, Rutgers University, New Jersey Medical School
- Jay H. Chung
- Laboratory of Obesity and Aging Research, Genetics and Development Biology Center, National Heart Lung and Blood Institute, National Institutes of Health
- DOI
- https://doi.org/10.1038/ncomms15560
- Journal volume & issue
-
Vol. 8,
no. 1
pp. 1 – 11
Abstract
The deacetylase Sirt1, known to regulate many cellular functions, can be activated by energy deprivation, however the mechanism is unclear. Here, the authors show that ATP inhibits Sirt1 by binding to the C-terminal domain, and energy deprivation derepresses Sirt1 activity by lowering the ATP level.
