Deletion of PRKAA triggers mitochondrial fission by inhibiting the autophagy-dependent degradation of DNM1L
Open accessAbstract
PRKAA (protein kinase, AMP-activated, α catalytic subunit) regulates mitochondrial biogenesis, function, and turnover. However, the molecular mechanisms by which PRKAA regulates mitochondrial dynamics remain poorly characterized. Here, we report that PRKAA regulated mitochondrial fission via the autophagy-dependent degradation of DNM1L (dynamin 1-like). Deletion of Prkaa1/AMPKα1 or Prkaa2/AMPKα2 resulted in defective autophagy, DNM1L accumulation, and aberrant mitochondrial fragmentation in the mouse aortic endothelium. Furthermore, autophagy inhibition by chloroquine treatment or ATG7 small interfering RNA (siRNA) transfection, upregulated DNM1L expression and triggered DNM1L-mediated mitochondrial fragmentation. In contrast, autophagy activation by overexpression of ATG7 or chronic administration of rapamycin, the MTOR inhibitor, promoted DNM1L degradation and attenuated mitochondrial fragmentation in Prkaa2-deficient (prkaa2−/−) mice, suggesting that defective autophagy contributes to enhanced DNM1L expression and mitochondrial fragmentation. Additionally, the autophagic receptor protein SQSTM1/p62, which bound to DNM1L and led to its translocation into the autophagosome, was involved in DNM1L degradation by the autophagy-lysosome pathway. Gene silencing of SQSTM1 markedly reduced the association between SQSTM1 and DNM1L, impaired the degradation of DNM1L, and enhanced mitochondrial fragmentation in PRKAA-deficient endothelial cells. Finally, the genetic (DNM1L siRNA) or pharmacological (mdivi-1) inhibition of DNMA1L ablated mitochondrial fragmentation in the mouse aortic endothelium and prevented the acetylcholine-induced relaxation of isolated mouse aortas. This suggests that aberrant DNM1L is responsible for enhanced mitochondrial fragmentation and endothelial dysfunction in prkaa knockout mice. Overall, our results show that PRKAA deletion promoted mitochondrial fragmentation in vascular endothelial cells by inhibiting the autophagy-dependent degradation of DNM1L.
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AMPK deletion promoted mitochondrial fragmentation in endothelial cells by inhibiting the autophagy-dependent degradation of DRP1.
“Studies showed that AMPK deletion promoted mitochondrial fragmentation in ECs by inhibiting the autophagy-dependent degradation of DRP1 [105].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [105]
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- Authors
- Wang, Q., Wu, S., Zhu, H., Ding, Y., Dai, X., Ouyang, C., Han, Y.-M., Xie, Z., & Zou, M.-H.
- Affiliations
- Georgia State University (US)
- Corresponding author
- Xie, Zhonglin
- Zou, Ming-Hui
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2017-01-13
- Volume
- 13
- Issue
- 2
- Pages
- 404-422
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC5324848
- OpenAlex
- W2577260066
- Cited by
- 45
- References
- 62
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 8 · 2023: 4 · 2022: 6 · 2021: 6 · 2020: 8 · 2019: 2 · 2018: 3 · 2017: 2
- FWCI
- 3.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HL080499, HL137371)
- National Institute on Aging (R01AG047776)
- National Heart, Lung, and Blood Institute (R01HL079584, R01HL132500, R01HL110488, R01HL089920)
- National Cancer Institute (R01CA213022)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- AMPK, Drp1, mitochondrial fission, mitochondrial fragmentation, p62, autophagosomes, ATG7, Mdivi-1, endothelial dysfunction, aortic endothelium, vasorelaxation, acetylcholine
- MeSH terms
- Sequestosome-1 Protein, Animals, Aorta, Autophagy, Cell Separation, Endothelium, Vascular, Humans, Mice, Inbred C57BL, Microtubule-Associated Proteins, Phosphorylation, Phosphoserine, Vasodilation, Gene Deletion, Sirolimus, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, AMP-Activated Protein Kinases, Proteolysis, Human Umbilical Vein Endothelial Cells, Mitochondrial Dynamics
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