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SIRT1 deacetylates mitochondrial trifunctional enzyme α subunit to inhibit ubiquitylation and decrease insulin

Yan-Mei Wang1, Ting-Lei Huang2, Chao Meng1

  • 1Department of Geriatrics, Ren Ji Hospital, School of Medicine, Shanghai Jiao Tong University, No. 160 Pujian Road, Pudong New Area, Shanghai, 200127, China.

Cell Death & Disease
|October 3, 2020
PubMed
Summary
This summary is machine-generated.

Mitochondrial trifunctional enzyme subunit alpha (MTPα) enhances glucose uptake and lowers blood sugar, revealing its potential in combating insulin resistance and diabetes. Its stability, regulated by deacetylation, is key to metabolic health.

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Area of Science:

  • Metabolic regulation
  • Molecular biology
  • Diabetes research

Background:

  • Insulin resistance and diabetes are linked to disrupted free fatty acid metabolism.
  • Mitochondrial trifunctional enzyme subunit alpha (MTPα) is involved in fatty acid oxidation, but its role in insulin resistance is unclear.

Purpose of the Study:

  • To investigate the effect of MTPα on insulin resistance.
  • To explore the molecular mechanisms regulating MTPα activity and stability.

Main Methods:

  • Studied MTPα in insulin-resistant 3T3-L1 adipocytes and db/db diabetic mice.
  • Utilized quantitative real-time PCR, immunoblotting, and immunoprecipitation.
  • Assessed acetylation and ubiquitylation modifications of MTPα.

Main Results:

  • MTPα overexpression increased glucose uptake via Glut4 translocation in adipocytes.
  • Upregulated MTPα reduced blood glucose levels in diabetic mice.
  • Deacetylation enhanced MTPα stability and insulin-sensitizing effects, with SIRT1 activation preventing MTPα degradation.

Conclusions:

  • MTPα plays a novel role in ameliorating insulin resistance.
  • Acetylation and ubiquitylation are critical regulators of MTPα function in glucose metabolism.