The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Transient assembly of F-actin on the outer mitochondrial membrane contributes to mitochondrial fission
Open accessAbstract
In addition to established membrane remodeling roles in various cellular locations, actin has recently emerged as a participant in mitochondrial fission. However, the underlying mechanisms of its participation remain largely unknown. We report that transient de novo F-actin assembly on the mitochondria occurs upon induction of mitochondrial fission and F-actin accumulates on the mitochondria without forming detectable submitochondrial foci. Impairing mitochondrial division through Drp1 knockout or inhibition prolonged the time of mitochondrial accumulation of F-actin and also led to abnormal mitochondrial accumulation of the actin regulatory factors cortactin, cofilin, and Arp2/3 complexes, suggesting that disassembly of mitochondrial F-actin depends on Drp1 activity. Furthermore, down-regulation of actin regulatory proteins led to elongation of mitochondria, associated with mitochondrial accumulation of Drp1. In addition, depletion of cortactin inhibited Mfn2 down-regulation– or FCCP-induced mitochondrial fragmentation. These data indicate that the dynamic assembly and disassembly of F-actin on the mitochondria participates in Drp1-mediated mitochondrial fission.
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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
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · cited 1×
“For example, mutations in Mfn2 (mitochondrial fusion factor Mitofusin 2) result in CMT2A (Charcot-Marie-Tooth Neuropathy type 2A; Züchner et al., 2004), an inherited disorder of the peripheral nervous system.”
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754
MiD49 and MiD51, new components of the mitochondrial fission machinery
Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T. (2011) · The EMBO Reports · doi:10.1038/embor.2011.54 · Cited by 649 · cited 6×
“…receptors of Drp1, or expression of a dominant-negative mutant of MARCH5, a mitochondria-associated E3 ubiquitin ligase, led to mitochondrial accumulation of Drp1 fission complexes associated with abnormal elongation of mitochondria (Karbowski et al., 2007; Palmer et al., 2011; Losón et al., 2013).”
InfluentialRole of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625
Self-citation
Cited by
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S. (2021) · The FASEB Journal · doi:10.1096/fj.202100067r · Cited by 733
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625
Zhou, H., Wang, S., Zhu, P., Hu, S., Chen, Y., & Ren, J. (2018) · Redox Biology · doi:10.1016/j.redox.2017.12.019 · Cited by 550
“Considering the indispensable nature of F-actin in fission [47,48], we argue that excessive fission would consume large amounts of cytoplasmic F-actin and also cause the uneven distribution of F-actin [46], ultimately resulting in the dysregulated F-actin homeostasis and impaired migration.”
BackgroundMitochondria and Reactive Oxygen Species in Aging and Age-Related Diseases
(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.006 · Cited by 455
Metadata
- Authors
- Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-12-29
- Volume
- 208
- Issue
- 1
- Pages
- 109-123
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1975251186
- Cited by
- 210
- References
- 14
- FWCI
- 6.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
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