Authors

Lu Liu, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Shuaiyi Chen, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Miao Yu, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Chenxu Ge, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Mengmeng Ren, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Boya Liu, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Xin Yang, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Thomas W Christian, Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, 220 BLSB, Philadelphia, PA 19107, United StatesFollow
Ya-Ming Hou, Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, 220 BLSB, Philadelphia, PA 19107, United StatesFollow
Junhua Zou, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China
Wei-Guo Zhu, Department of Biochemistry and Molecular Biology, Shenzhen University School of Medicine, Shenzhen, 518060, China
Jianyuan Luo, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing, 100191, China; Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing, 100191, China

Document Type

Article

Publication Date

7-23-2020

Comments

This article has been peer reviewed. It was published in: Cell Death and Disease.

Volume 11, Issue 7, 1 July 2020, Article number 563.

The published version is available at DOI: 10.1038/s41419-020-02763-9

Copyright © The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

Abstract

17-beta-hydroxysteroid dehydrogenase 10 (HSD17B10) plays an important role in mitochondrial fatty acid metabolism and is also involved in mitochondrial tRNA maturation. HSD17B10 missense mutations cause HSD10 mitochondrial disease (HSD10MD). HSD17B10 with mutations identified from cases of HSD10MD show loss of function in dehydrogenase activity and mitochondrial tRNA maturation, resulting in mitochondrial dysfunction. It has also been implicated to play roles in the development of Alzheimer disease (AD) and tumorigenesis. Here, we found that HSD17B10 is a new substrate of NAD-dependent deacetylase Sirtuin 3 (SIRT3). HSD17B10 is acetylated at lysine residues K79, K99 and K105 by the acetyltransferase CBP, and the acetylation is reversed by SIRT3. HSD17B10 acetylation regulates its enzymatic activity and the formation of mitochondrial RNase P. Furthermore, HSD17B10 acetylation regulates the intracellular functions, affecting cell growth and cell resistance in response to stresses. Our results demonstrated that acetylation is an important regulation mechanism for HSD17B10 and may provide insight into interrupting the development of AD.

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

PubMed ID

32703935

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