Cited by 1,270Mitochondrial Function and PathologyCell death mechanisms and regulationAutophagy in Disease and Therapy

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Mitochondrial dynamics and apoptosis

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Suen, Der-Fen, Norris, Kristi L., Youle, Richard J.·2008·Genes & Development

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Abstract

In healthy cells, mitochondria continually divide and fuse to form a dynamic interconnecting network. The molecular machinery that mediates this organelle fission and fusion is necessary to maintain mitochondrial integrity, perhaps by facilitating DNA or protein quality control. This network disintegrates during apoptosis at the time of cytochrome c release and prior to caspase activation, yielding more numerous and smaller mitochondria. Recent work shows that proteins involved in mitochondrial fission and fusion also actively participate in apoptosis induction. This review will cover the recent advances and presents competing models on how the mitochondrial fission and fusion machinery may intersect apoptosis pathways.

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Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806
Self-citation
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
Vaux, D., Cory, S., & Adams, J. (1988) · Nature · doi:10.1038/335440a0 · Cited by 3,355
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
The Bcl-2 apoptotic switch in cancer development and therapy
Adams, J. M., & Cory, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210220 · Cited by 2,256
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
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Authors: Suen, D.-F., Norris, K. L., & Youle, R. J.
Affiliations: National Institutes of Health (US)
ORCID: Suen, Der-Fen
Youle, Richard J.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2008-06-15
Volume: 22
Issue: 12
Pages: 1577-1590
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.1658508
PMC: PMC2732420
OpenAlex: W2104954806
Cited by: 1,270
References: 209
Citations by year: 2026: 27 · 2025: 41 · 2024: 62 · 2023: 65 · 2022: 57 · 2021: 84 · 2020: 81 · 2019: 69 · 2018: 82 · 2017: 86 · 2016: 95 · 2015: 79 · 2014: 89 · 2013: 63 · 2012: 75
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, apoptosis, cytochrome c release, caspase activation, mitochondrial quality control, mitochondrial network, apoptosis induction
MeSH terms: Animals, Cell Division, Cell Fusion, Humans, Membrane Proteins, Mitochondria, Models, Biological, Protein Processing, Post-Translational, Cellular Senescence, Apoptosis, Calcium-Calmodulin-Dependent Protein Kinases, Proto-Oncogene Proteins c-bcl-2, GTP Phosphohydrolases, Mitochondrial Proteins, Drosophila Proteins, Cytochromes c, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Death-Associated Protein Kinases

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