Mitochondrial dynamics in adaptive and maladaptive cellular stress responses

Eisner, Verónica; Picard, Martin; Hajnóczky, György

doi:10.1038/s41556-018-0133-0

Cited by 623Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

Mitochondrial dynamics in adaptive and maladaptive cellular stress responses

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Eisner, Verónica, Picard, Martin, Hajnóczky, György·2018·Nature Cell Biology

DOI 10.1038/s41556-018-0133-0PMC PMC6716149

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During mitochondrial fission, cytosolic Drp1 is recruited to mitochondrial receptors (e.g., Fis1), allowing mitochondrial partitioning, turnover and reduction of network size under low energetic demand.
“During mitochondrial fission, cytosolic Drp1 is recruited to mitochondrial receptors (e.g., Fis1)3,4, allowing mitochondrial partitioning, turnover and reduction of network size under low energetic demand4,7.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [3]
The “Mitochondrial fusion and fission dynamics” section (page unavailable) describes cytoplasmic DRP1 recruitment for division and says fission enables segregation of damaged mitochondria for mitophagy. It names MFF and MID49/51, not Fis1, in the recruitment mechanism. It also does not establish that low energetic demand drives network reduction; its discussion of glucose starvation instead describes inhibited fission and hyperfusion. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Mitochondrial dysfunction is not a consistent biomarker of senescence because it characterizes other cellular processes.
“Because mitochondrial dysfunction characterizes other cellular processes (Eisner et al., 2018), it is not a consistent biomarker of senescence.”
From Cellular Senescence: Defining a Path Forward (2019) · cites this paper as Eisner et al., 2018
Several proteins are required for mitochondrial fusion, including the mitofusins (Mfn1/Mfn2).
“Several proteins are required for mitochondrial fusion, including the mitofusins (Mfn1/Mfn2)3,4.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [3]
Mitochondrial dynamics include fusion, fission, and degradation events, linked to mitochondrial function.
“Mitochondrial dynamics include fusion, fission, and degradation events, linked to mitochondrial function3,4.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [3]
Mitochondrial fusion is mediated by mitofusins, which are regulated by transcription and protein modification, including ubiquitination.
“Mitochondrial fusion is mediated by mitofusins, which are regulated by transcription and protein modification, including ubiquitination3.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [3]

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Mice Hemizygous for a Pathogenic Mitofusin-2 Allele Exhibit Hind Limb/Foot Gait Deficits and Phenotypic Perturbations in Nerve and Muscle
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Cellular Senescence: Defining a Path Forward
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The cell biology of mitochondrial membrane dynamics
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Multifaceted mitochondria: moving mitochondrial science beyond function and dysfunction
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A pipeline for multidimensional confocal analysis of mitochondrial morphology, function, and dynamics in pancreatic β-cells
Chaudhry, A., Shi, R., & Luciani, D. S. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00457.2019 · Cited by 435 · see citing works
Drp1-dependent mitochondrial fission in cardiovascular disease
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Mitochondria as central hub of the immune system
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Mitochondrial metabolism regulates macrophage biology
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Mitochondria dysfunction and metabolic reprogramming as drivers of idiopathic pulmonary fibrosis
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Pleiotropic effects of mitochondria in aging
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Mitophagy in Human Diseases
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Mitochondrial Structure and Function in Human Heart Failure
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Transmission Electron Microscopy as a Powerful Tool to Investigate the Interaction of Nanoparticles with Subcellular Structures
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Outstanding Questions in Mitophagy: What We Do and Do Not Know
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Mitochondrial protein-induced stress triggers a global adaptive transcriptional programme
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Tau accumulation in astrocytes of the dentate gyrus induces neuronal dysfunction and memory deficits in Alzheimer’s disease
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Mitophagy: Molecular Mechanisms, New Concepts on Parkin Activation and the Emerging Role of AMPK/ULK1 Axis
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Autophagy in cancer development, immune evasion, and drug resistance
Niu, X., You, Q., Hou, K., Tian, Y., Wei, P., Zhu, Y., Gao, B., Ashrafizadeh, M., Aref, A. R., Kalbasi, A., et al. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101170 · Cited by 217 · see citing works
Quantitative 3D Mapping of the Human Skeletal Muscle Mitochondrial Network
Vincent, A. E., White, K., Davey, T., Philips, J., Ogden, R. T., Lawless, C., Warren, C., Hall, M. G., Ng, Y. S., Falkous, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.010 · Cited by 195 · see citing works
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Metabolic reprogramming in osteoclasts
Park‐Min, K. (2019) · Seminars in Immunopathology · doi:10.1007/s00281-019-00757-0 · Cited by 196 · see citing works
BNIP3L/NIX-mediated mitophagy protects against glucocorticoid-induced synapse defects
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The Good and the Bad of Mitochondrial Breakups
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Emerging role of mitophagy in cardiovascular physiology and pathology
Morales, P. E., Arias-Durán, C., Ávalos-Guajardo, Y., Aedo, G., Verdejo, H., Parra, V., & Lavandero, S. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.09.006 · Cited by 178 · see citing works
Mitochondrial morphology controls fatty acid utilization by changing CPT1 sensitivity to malonyl‐CoA
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Is Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
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Mitochondrial quality control: from molecule to organelle
Roca-Portoles, A., & Tait, S. W. G. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03775-0 · Cited by 174 · see citing works
PINK1-Mediated Mitophagy Promotes Oxidative Phosphorylation and Redox Homeostasis to Induce Drug-Tolerant Persister Cancer Cells
Li, Y., Chen, H., Xie, X., Yang, B., Wang, X., Zhang, J., Qiao, T., Guan, J., Qiu, Y., Huang, Y., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-2370 · Cited by 175 · see citing works
SIRT3-Dependent Mitochondrial Dynamics Remodeling Contributes to Oxidative Stress-Induced Melanocyte Degeneration in Vitiligo
Yi, X., Guo, W., Shi, Q., Yang, Y., Zhang, W., Chen, X., Kang, P., Chen, J., Cui, T., Ma, J., et al. (2019) · Theranostics · doi:10.7150/thno.30398 · Cited by 167 · see citing works
Mitochondrial Dynamics: Fission and Fusion in Fate Determination of Mesenchymal Stem Cells
Ren, L., Chen, X., Chen, X., Li, J., Cheng, B., & Xia, J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.580070 · Cited by 165 · see citing works
Mitochondrial Oxidative Stress and “Mito-Inflammation”: Actors in the Diseases
Patergnani, S., Bouhamida, E., Leo, S., Pinton, P., & Rimessi, A. (2021) · Biomedicines · doi:10.3390/biomedicines9020216 · Cited by 172 · see citing works
Mitochondrial dynamics and mitophagy in lung disorders
Sharma, A. K., Ahmad, S., Ahmad, T., Ali, S., & Syed, M. A. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119876 · Cited by 157 · see citing works
Denervation drives skeletal muscle atrophy and induces mitochondrial dysfunction, mitophagy and apoptosis via miR-142a-5p/MFN1 axis
Yang, X., Xue, P., Chen, H., Yuan, M., Kang, Y., Duscher, D., Machens, H., & Chen, Z. (2020) · Theranostics · doi:10.7150/thno.40857 · Cited by 147 · see citing works
Glaucomatous optic neuropathy: Mitochondrial dynamics, dysfunction and protection in retinal ganglion cells
Ju, W., Perkins, G. A., Keun-young Kim, A., Bastola, T., Choi, W.-Y., & Choi, S. (2022) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2022.101136 · Cited by 148 · see citing works
The Overcrowded Crossroads: Mitochondria, Alpha-Synuclein, and the Endo-Lysosomal System Interaction in Parkinson’s Disease
Lin, K.-J., Lin, K.-L., Chen, S., Liou, C., Chuang, Y., Lin, H., & Lin, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215312 · Cited by 141 · see citing works
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 141 · see citing works
A break in mitochondrial endosymbiosis as a basis for inflammatory diseases
Murphy, M. P., & O’Neill, L. A. J. (2024) · Nature · doi:10.1038/s41586-023-06866-z · Cited by 138 · see citing works
Structural mechanism of mitochondrial membrane remodelling by human OPA1
von der Malsburg, A., Sapp, G., Zuccaro, K. E., von Appen, A., Moss, F. R., Kalia, R., Bennett, J. A., Abriata, L. A., Peraro, M. D., van der Laan, M., et al. (2023) · Nature · doi:10.1038/s41586-023-06441-6 · Cited by 144 · see citing works
Fibroblast growth factor 18 exerts anti-osteoarthritic effects through PI3K-AKT signaling and mitochondrial fusion and fission
Yao, X., Zhang, J., Jing, X., Ye, Y., Guo, J., Sun, K., & Guo, F. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.026 · Cited by 134 · see citing works
Nuclear-Mitochondrial Interactions
Walker, B. R., & Moraes, C. T. (2022) · Biomolecules · doi:10.3390/biom12030427 · Cited by 136 · see citing works
Motion of VAPB molecules reveals ER–mitochondria contact site subdomains
Obara, C. J., Nixon‐Abell, J., Moore, A. S., Riccio, F., Hoffman, D. P., Shtengel, G. E., Xu, C. S., Schaefer, K., Pasolli, H. A., Masson, J., et al. (2024) · Nature · doi:10.1038/s41586-023-06956-y · Cited by 130 · see citing works
Dendrobium officinale polysaccharide triggers mitochondrial disorder to induce colon cancer cell death via ROS-AMPK-autophagy pathway
Zhang, K., Zhou, X., Wang, J., Zhou, Y., Qi, W., Chen, H., Nie, S., & Xie, M. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118018 · Cited by 128 · see citing works
Mitochondrial complex I as a therapeutic target for Alzheimer's disease
Trushina, E. V., Trushin, S., & Hasan, M. F. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.11.003 · Cited by 130 · see citing works
The roles of mitochondria in global and local intracellular calcium signalling
Cartes-Saavedra, B., Ghosh, A., & Hajnóczky, G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00820-1 · Cited by 126 · see citing works
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Altered mitochondrial dynamics and function in APOE4-expressing astrocytes
Schmukler, E., Solomon, S., Simonovitch, S., Goldshmit, Y., Wolfson, E., Michaelson, D. M., & Pinkas-Kramarski, R. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-02776-4 · Cited by 125 · see citing works
Differential Effects of Oleic and Palmitic Acids on Lipid Droplet-Mitochondria Interaction in the Hepatic Cell Line HepG2
Eynaudi, A., Díaz-Castro, F., Bórquez, J. C., Bravo-Sagua, R., Parra, V., & Troncoso, R. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.775382 · Cited by 125 · see citing works
Determinants, maintenance, and function of organellar pH
Freeman, S. A., Grinstein, S., & Orlowski, J. (2022) · Physiological Reviews · doi:10.1152/physrev.00009.2022 · Cited by 127 · see citing works
Mitochondrial Heterogeneity
Aryaman, J., Johnston, I. G., & Jones, N. S. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2018.00718 · Cited by 121 · see citing works
The Balance of MFN2 and OPA1 in Mitochondrial Dynamics, Cellular Homeostasis, and Disease
Zanfardino, P., Amati, A., Perrone, M., & Petruzzella, V. (2025) · Biomolecules · doi:10.3390/biom15030433 · Cited by 125 · see citing works
Posttranslational modifications of mitochondrial fission and fusion proteins in cardiac physiology and pathophysiology
Adaniya, S. M., O‐Uchi, J., Cypress, M. W., Kusakari, Y., & Jhun, B. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00523.2018 · Cited by 115 · see citing works
The right time for senescence
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Physical Exercise: A Novel Tool to Protect Mitochondrial Health
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BNIP3L/Nix-induced mitochondrial fission, mitophagy, and impaired myocyte glucose uptake are abrogated by PRKA/PKA phosphorylation
da Silva Rosa, S. C., Martens, M. D., Field, J. T., Nguyen, L., Kereliuk, S. M., Hai, Y., Chapman, D., Diehl-Jones, W., Aliani, M., West, A. R., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1821548 · Cited by 117 · see citing works
Role of Mitochondria in Viral Infections
Elesela, S., & Lukacs, N. W. (2021) · Life · doi:10.3390/life11030232 · Cited by 113 · see citing works
Muscle-generated BDNF (brain derived neurotrophic factor) maintains mitochondrial quality control in female mice
Ahuja, P., Ng, C. F., Pang, B. P. S., Chan, W. S., Tse, M. C. L., Bi, X., Kwan, H.-L. R., Brobst, D., Herlea-Pana, O., Yang, X., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1985257 · Cited by 116 · see citing works
Succinyl-CoA Ligase Deficiency in Pro-inflammatory and Tissue-Invasive T Cells
Wu, B., Qiu, J., Zhao, T. V., Wang, Y., Maeda, T., Goronzy, I. N., Akiyama, M., Ohtsuki, S., Jin, K., Tian, L., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.025 · Cited by 112 · see citing works
Metformin alleviates lead-induced mitochondrial fragmentation via AMPK/Nrf2 activation in SH-SY5Y cells
Yang, L., Li, X., Jiang, A., Li, X., Chang, W., Chen, J., & Ye, F. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101626 · Cited by 110 · see citing works
ER-mitochondria contacts promote mtDNA nucleoids active transportation via mitochondrial dynamic tubulation
Qin, J., Guo, Y., Xue, B., Shi, P., Yang, C., Su, Q. P., Hao, H., Zhao, S., Wu, C., Yu, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18202-4 · Cited by 110 · see citing works
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Authors: Eisner, V., Picard, M., & Hajnóczky, G.
Affiliations: Pontificia Universidad Católica de Chile (CL)
Columbia University Irving Medical Center (US)
Thomas Jefferson University (US)
Corresponding author: Hajnóczky, György
ORCID: Eisner, Verónica
Picard, Martin
Hajnóczky, György
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2018-06-27
Volume: 20
Issue: 7
Pages: 755-765
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/s41556-018-0133-0
PMC: PMC6716149
OpenAlex: W2809177340
Cited by: 622
References: 180
Citations by year: 2026: 63 · 2025: 78 · 2024: 83 · 2023: 86 · 2022: 81 · 2021: 93 · 2020: 87 · 2019: 44 · 2018: 5 · 2016: 1
FWCI: 5.62
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Americanae (AECID Library) (submittedVersion, cc-by-nc-nd)
LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, cc-by-nc-nd)
Funders: National Institute on Alcohol Abuse and Alcoholism (U01AA021122)
National Institute of Mental Health (R21MH113011)
National Institute of General Medical Sciences (R35GM119793)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK051526)
National Institute of Environmental Health Sciences (R33ES025672)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: mitochondrial dynamics, mitochondrial fusion, mitochondrial fission, mitochondrial motility, endoplasmic reticulum-mitochondria interaction, cellular stress response, adaptive stress response, maladaptive stress response, cell survival and death, energy production, mitochondrial signalling, mitochondrial disease
MeSH terms: Adaptation, Physiological, Animals, Cell Survival, Energy Metabolism, Humans, Mitochondria, Stress, Physiological, Signal Transduction, Cell Death, Mitochondrial Dynamics

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