{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu L"],"funding":["NIA NIH HHS","NIAID NIH HHS","National Natural Science Foundation of China","NIGMS NIH HHS"],"pagination":["563"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7378191"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(7)"],"pubmed_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."],"journal":["Cell death & disease"],"pubmed_title":["Deacetylation of HSD17B10 by SIRT3 regulates cell growth and cell resistance under oxidative and starvation stresses."],"pmcid":["PMC7378191"],"funding_grant_id":["R01 GM126210","81621063","R01 GM114343","R35 GM134931","R21 AG042169","81874147","81671389","R01 AI139202"],"pubmed_authors":["Ge C","Yang X","Zou J","Yu M","Liu L","Luo J","Christian TW","Hou YM","Liu B","Zhu WG","Ren M","Chen S"],"additional_accession":[]},"is_claimable":false,"name":"Deacetylation of HSD17B10 by SIRT3 regulates cell growth and cell resistance under oxidative and starvation stresses.","description":"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.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jul","modification":"2024-12-03T18:38:45.804Z","creation":"2024-12-03T18:38:45.804Z"},"accession":"S-EPMC7378191","cross_references":{"pubmed":["32703935"],"doi":["10.1038/s41419-020-02763-9"]}}