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Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells
Open accessAbstract
Recognition of injured mitochondria for degradation by macroautophagy is essential for cellular health, but the mechanisms remain poorly understood. Cardiolipin is an inner mitochondrial membrane phospholipid. We found that rotenone, staurosporine, 6-hydroxydopamine and other pro-mitophagy stimuli caused externalization of cardiolipin to the mitochondrial surface in primary cortical neurons and SH-SY5Y cells. RNAi knockdown of cardiolipin synthase or of phospholipid scramblase-3, which transports cardiolipin to the outer mitochondrial membrane, decreased the delivery of mitochondria to autophagosomes. Furthermore, we found that the autophagy protein microtubule-associated-protein-1 light chain 3 (LC3), which mediates both autophagosome formation and cargo recognition, contains cardiolipin-binding sites important for the engulfment of mitochondria by the autophagic system. Mutation of LC3 residues predicted as cardiolipin-interaction sites by computational modelling inhibited its participation in mitophagy. These data indicate that redistribution of cardiolipin serves as an 'eat-me' signal for the elimination of damaged mitochondria from neuronal cells.
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In the citing paper
“changes in LC3-II amounts are tissue- and cell context-dependent.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“In the absence of lysosomal protease inhibitors, starvation results in a modest increase (HEK 293 cells) or even a decrease (HeLa cells) in the amount of LC3-II. The use of inhibitors reveals that this apparent decrease is due to lysosome-dependent degradation.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredIn the citing paper
“Cardiolipin — a phospholipid that is normally segregated to the inner mitochondrial membrane and is essential to the maintenance of mitochondrial architecture and function — when herniated outside a damaged mitochondrial membrane, stimulates mitophagy, a process that eliminates dysfunctional mitochondria and promotes the formation of new mitochondria (79).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [79]
In the citing paper
“It should also be mentioned that the translocation of cardiolipin from the inner to outer mitochondrial membrane is another event that can trigger mitophagy [144].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [144]
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“LC3 proteins are involved in autophagosome formation, with participation of GABARAP subfamily members in later stages of autophagosome formation [201].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [201]
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Metadata
- Authors
- Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., Qiang Wang, K. Z., Zhu, J., Klein-Seetharaman, J., Balasubramanian, K., Amoscato, A. A., Borisenko, G., Huang, Z., Gusdon, A. M., Cheikhi, A., Steer, E. K., Wang, R., Baty, C., Watkins, S., Bahar, I., Bayır, H., & Kagan, V. E.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Chu, Charleen T.
- Tyurina, Yulia Y.
- Bayır, Hülya
- Kagan, Valerian E.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2013-09-15
- Volume
- 15
- Issue
- 10
- Pages
- 1197-1205
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3806088
- OpenAlex
- W2135592618
- Cited by
- 1,083
- References
- 66
- Citations by year
- 2026: 75 · 2025: 96 · 2024: 102 · 2023: 87 · 2022: 83 · 2021: 105 · 2020: 104 · 2019: 82 · 2018: 73 · 2017: 85 · 2016: 60 · 2015: 65 · 2014: 59 · 2013: 6
- FWCI
- 46.15
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (U19AIO68021)
- National Institute on Aging (AG026389, F32AG030821, R01AG026389)
- National Heart, Lung, and Blood Institute (HL-70755, R01HL070755, R01HL094488)
- National Institute of General Medical Sciences (P20GM103554, P41GM103712)
- National Institute of Allergy and Infectious Diseases (U19AI068021)
- National Institute of Neurological Disorders and Stroke (NS065789, NS076511, R01NS061817, R01NS065789, NS061817, R56NS065789, R37NS061817, R01NS076511)
- National Institute of Environmental Health Sciences (R21ES021068, ES 020693, R01ES020693)
- National Institute for Occupational Safety and Health (R01 OH008282, OH008282)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R21HD057587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- cardiolipin, mitophagy, mitochondrial outer membrane, LC3, cardiolipin synthase, autophagy, neurons, mitochondrial damage, autophagosome formation, rotenone, staurosporine, 6-hydroxydopamine
- MeSH terms
- Amino Acid Sequence, Animals, Autophagy, Biological Transport, Cardiolipins, Cells, Cultured, HeLa Cells, Humans, Mitochondria, Models, Molecular, Molecular Sequence Data, Neurons, Rotenone, Uncoupling Agents, Signal Transduction, Oxidopamine, Rats, Sprague-Dawley, Protein Structure, Tertiary, Cell Line, Tumor, Mitochondrial Membranes, Rats, Gene Knockdown Techniques, Mitophagy
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