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A link between protein acetylation and mitochondrial dynamics under energy metabolism: A comprehensive overview

Journal

JOURNAL OF CELLULAR PHYSIOLOGY
Volume 236, Issue 12, Pages 7926-7937

Publisher

WILEY
DOI: 10.1002/jcp.30461

Keywords

energy metabolism; mitochondrial dynamics; protein acetylation

Funding

  1. Fundamental Research Funds for the Central Universities [Z1090219144]
  2. Key Sci-tech innovation team of Shaanxi province [245201971]
  3. Joint Funds of the National Natural Science Foundation of China [U1804106]
  4. Natural Science Foundation of China [81860762]
  5. Scientific Research Guiding Plan Topic of Qinghai Hygiene Department [2018-wjzdx-131]
  6. Qinghai Fundamental Scientific and Technological Research Plan [2018-ZJ-721]

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Cells adjust mitochondrial morphologies through the balance between fusion and fission processes, regulated mainly by posttranslational modifications. More than 20% of mitochondrial proteins are acetylated and play a role in the dynamic regulation of fusion and fission.
Cells adjust mitochondrial morphologies to coordinate between the cellular demand for energy and the availability of resources. Mitochondrial morphology is regulated by the balance between two counteracting mitochondrial processes of fusion and fission. Fission and fusion are dynamic and reversible processes that depend on the coordination of a number of proteins and are primarily regulated by posttranslational modifications. In the mitochondria, more than 20% of proteins are acetylated in proteomic surveys, partly involved in the dynamic regulation of mitochondrial fusion and fission. This article focuses on the molecular mechanism of the mitochondrial dynamics of fusion and fission, and summarizes the related mechanisms and targets of mitochondrial protein acetylation to regulate the mitochondrial dynamics of fusion and fission in energy metabolism.

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