Unknown

Dataset Information

0

The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to ?-cell function.


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 ?-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 ?-cells. SIRT3 expression was upregulated in rat islets upon exposure to low glucose or fasting. SIRT3 overexpression in islets markedly decreased palmitate-potentiated insulin secretion, whereas islets from SIRT3 knockout mice secreted more insulin, with an opposite action on FAO. ECHA overexpression partially reversed SIRT3 deficiency-elicited insulin hypersecretion. Our study highlights the potential role of protein acetylation in insulin secretion.

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC6347623 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function.

Zhang Yuqing Y   Zhou Feiye F   Bai Mengyao M   Liu Yun Y   Zhang Linlin L   Zhu Qin Q   Bi Yufang Y   Ning Guang G   Zhou Libin L   Wang Xiao X  

Cell death & disease 20190125 2


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  ...[more]

Similar Datasets

| S-EPMC8409982 | biostudies-literature
| S-EPMC7696085 | biostudies-literature
| S-EPMC9932481 | biostudies-literature
| S-EPMC10772559 | biostudies-literature
| S-EPMC6788807 | biostudies-literature
| S-EPMC10074109 | biostudies-literature
| S-EPMC6026123 | biostudies-literature
| S-EPMC9589032 | biostudies-literature
| S-EPMC4536436 | biostudies-literature
2024-09-10 | GSE275438 | GEO