MiD49 and MiD51, new components of the mitochondrial fission machinery
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Mitochondria form intricate networks through fission and fusion events. Here, we identify mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) anchored in the mitochondrial outer membrane. MiD49/51 form foci and rings around mitochondria similar to the fission mediator dynamin-related protein 1 (Drp1). MiD49/51 directly recruit Drp1 to the mitochondrial surface, whereas their knockdown reduces Drp1 association, leading to unopposed fusion. Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin. Thus, MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondria.
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MFF, MIEF2/MiD49, and MIEF1/MiD51 bind to DRP1 and arrange assembly of DRP1 oligomers at constriction sites.
“Instead, it has been reported that other components of the mammalian fission bind to DRP1 and arrange the assembly of DRP1 oligomers at constriction sites: mitochondrial fission factor (MFF), mitochondrial elongation factor 2/mitochondrial dynamics protein 49 (MIEF2/MiD49), and MIEF1/MiD51 [90–93].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [91]
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- Authors
- Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T.
- Affiliations
- La Trobe University (AU)
- Corresponding author
- Ryan, Michael T
- Venue
- The EMBO Reports
- Published
- 2011-04-21
- Volume
- 12
- Issue
- 6
- Pages
- 565-573
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC3128275
- OpenAlex
- W2005607645
- Cited by
- 649
- References
- 32
- Citations by year
- 2026: 18 · 2025: 34 · 2024: 40 · 2023: 36 · 2022: 48 · 2021: 63 · 2020: 56 · 2019: 47 · 2018: 44 · 2017: 48 · 2016: 45 · 2015: 48 · 2014: 43 · 2013: 45 · 2012: 24
- FWCI
- 15.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Medical Research Council
- National Health and Medical Research Council
- 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
- MiD51, mitochondrial fission, mitochondrial dynamics, Drp1, mitochondrial outer membrane, mitochondrial fusion, actin, mitochondrial division, dynamin-related proteins
- MeSH terms
- Actins, Amino Acid Sequence, Animals, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Cell Line, Chlorocebus aethiops, HeLa Cells, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Peptide Elongation Factors, Uncoupling Agents, Sequence Alignment, Receptors, Cytoplasmic and Nuclear, COS Cells, Protein Transport, Mitochondrial Proteins, RNA Interference, Mitochondrial Membranes, Mice, Membrane Potential, Mitochondrial
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