Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
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We find that Bax, a proapoptotic member of the Bcl-2 family, translocates to discrete foci on mitochondria during the initial stages of apoptosis, which subsequently become mitochondrial scission sites. A dominant negative mutant of Drp1, Drp1K38A, inhibits apoptotic scission of mitochondria, but does not inhibit Bax translocation or coalescence into foci. However, Drp1K38A causes the accumulation of mitochondrial fission intermediates that are associated with clusters of Bax. Surprisingly, Drp1 and Mfn2, but not other proteins implicated in the regulation of mitochondrial morphology, colocalize with Bax in these foci. We suggest that Bax participates in apoptotic fragmentation of mitochondria.
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Mitochondrial fusion is inhibited following MOMP, primarily due to repression of Mfn2 activity by Bax.
“It has been shown that mitochondrial fusion is inhibited following MOMP (Brooks et al., 2007), primarily due to repression of Mfn2 activity by Bax (Karbowski et al., 2002; Karbowski et al., 2006).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Karbowski et al., 2002
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References 25 · Cited by 846
Research works printed but not linked: 2
- Basanez, G., A. Nechushtan, O. Drozhinin, A. Chanturiya, E. Choe, S. Tutt, K. Wood, Y.-T. Hsu, J. Zimmerberg, and R.J. Youle. 1999. Full length Bax disrupts planar phospholipid membranes. Proc. Natl. Acad. Sci. USA. 96: 5492–5497. 10318911 PMC21887
- Hsu, Y.-T., K. Wolter, and R.J. Youle. 1997. Cytosol to membrane redistribution of members of the Bcl-2 family during apoptosis. Proc. Natl. Acad. Sci. USA. 94: 3668–3672. 9108035 PMC20498
- Authors
- Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Swiss National Bank (CH)
- Stanford Medicine (US)
- ORCID
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2002-12-23
- Volume
- 159
- Issue
- 6
- Pages
- 931-938
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2173996
- OpenAlex
- W2128347259
- Cited by
- 846
- References
- 25
- Citations by year
- 2026: 11 · 2025: 22 · 2024: 22 · 2023: 34 · 2022: 24 · 2021: 34 · 2020: 36 · 2019: 36 · 2018: 38 · 2017: 37 · 2016: 32 · 2015: 37 · 2014: 39 · 2013: 42 · 2012: 44
- FWCI
- 10.92
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Bax, mitochondrial fission, Drp1, mitofusin 2, apoptosis, mitochondrial morphology, Bcl-2 family proteins, Bax translocation, dominant-negative mutant, mitochondrial fragmentation
- MeSH terms
- Animals, Cell Survival, Cytoskeletal Proteins, Genes, Dominant, HeLa Cells, Humans, Immunohistochemistry, Membrane Proteins, Microscopy, Electron, Microscopy, Fluorescence, Mitochondria, Mutation, Plasmids, Proto-Oncogene Proteins, Subcellular Fractions, Time Factors, Transfection, Immunoblotting, Apoptosis, Protein Structure, Tertiary, DNA, Complementary, Microscopy, Confocal, Proto-Oncogene Proteins c-bcl-2, COS Cells, GTP Phosphohydrolases, Mitochondrial Proteins, Utrophin, bcl-2-Associated X Protein
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