{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["National Natural Science Foundation of China"],"pagination":["66"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6347623"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(2)"],"pubmed_abstract":["Protein acetylation has a crucial role in energy metabolism. Here we performed the first large-scale profiling of acetylome in rat islets, showing that almost all enzymes in core metabolic pathways related to insulin secretion were acetylated. Label-free quantitative acetylome of islets in response to high glucose revealed hyperacetylation of enzymes involved in fatty acid β-oxidation (FAO), including trifunctional enzyme subunit alpha (ECHA). Acetylation decreased the protein stability of ECHA and its ability to promote FAO. The overexpression of SIRT3, a major mitochondrial deacetylase, prevented the degradation of ECHA via decreasing its acetylation level in β-cells. SIRT3 expression was upregulated in rat islets upon exposure to low glucose or fasting. SIRT3 overexpression in islets ma"],"journal":["Cell death & disease"],"pubmed_title":["The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function."],"pmcid":["PMC6347623"],"funding_grant_id":["81270910","81170720","81570693","81370876"],"pubmed_authors":["Liu Y","Zhou L","Zhang Y","Bai M","Zhou F","Zhang L","Wang X","Zhu Q","Ning G","Bi Y"],"additional_accession":[]},"is_claimable":false,"name":"The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function.","description":"Protein acetylation has a crucial role in energy metabolism. Here we performed the first large-scale profiling of acetylome in rat islets, showing that almost all enzymes in core metabolic pathways related to insulin secretion were acetylated. Label-free quantitative acetylome of islets in response to high glucose revealed hyperacetylation of enzymes involved in fatty acid β-oxidation (FAO), including trifunctional enzyme subunit alpha (ECHA). Acetylation decreased the protein stability of ECHA and its ability to promote FAO. The overexpression of SIRT3, a major mitochondrial deacetylase, prevented the degradation of ECHA via decreasing its acetylation level in β-cells. SIRT3 expression was upregulated in rat islets upon exposure to low glucose or fasting. SIRT3 overexpression in islets ma","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jan","modification":"2025-05-29T22:27:59.623Z","creation":"2025-05-29T22:27:59.623Z"},"accession":"S-EPMC6347623","cross_references":{"pubmed":["30683850"],"doi":["10.1038/s41419-019-1349-z"]}}