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Adaptor Proteins MiD49 and MiD51 Can Act Independently of Mff and Fis1 in Drp1 Recruitment and Are Specific for Mitochondrial Fission
Open accessAbstract
Drp1 (dynamin-related protein 1) is recruited to both mitochondrial and peroxisomal membranes to execute fission. Fis1 and Mff are Drp1 receptor/effector proteins of mitochondria and peroxisomes. Recently, MiD49 and MiD51 were also shown to recruit Drp1 to the mitochondrial surface; however, different reports have ascribed opposing roles in fission and fusion. Here, we show that MiD49 or MiD51 overexpression blocked fission by acting in a dominant-negative manner by sequestering Drp1 specifically at mitochondria, causing unopposed fusion events at mitochondria along with elongation of peroxisomes. Mitochondrial elongation caused by MiD49/51 overexpression required the action of fusion mediators mitofusins 1 and 2. Furthermore, at low level overexpression when MiD49 and MiD51 form discrete foci at mitochondria, mitochondrial fission events still occurred. Unlike Fis1 and Mff, MiD49 and MiD51 were not targeted to the peroxisomal surface, suggesting that they specifically act to facilitate Drp1-directed fission at mitochondria. Moreover, when MiD49 or MiD51 was targeted to the surface of peroxisomes or lysosomes, Drp1 was specifically recruited to these organelles. Moreover, the Drp1 recruitment activity of MiD49/51 appeared stronger than that of Mff or Fis1. We conclude that MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and suggest that they provide specificity to the division of mitochondria. Background: Various receptor proteins recruit Drp1 to drive fission of mitochondria and peroxisomes. Results: MiD49 and MiD51 recruit Drp1 specifically to mitochondria independently of receptors Fis1 and Mff. Conclusion: MiD49 and MiD51 appear to be specific to the mitochondrial fission apparatus of mammalian cells. Significance: Mitochondrial and peroxisomal fission processes can be differentially regulated.
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“MIEF1/MiD51 and the variant MIEF2/MiD49 recruit DRP1 to mitochondria independent of MFF, but in contrast to MFF, inhibit DRP1 GTPase activity leading to mitochondrial elongation when MiD49/51 is overexpressed [92, 95, 96].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [92]
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“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 [92]
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Metadata
- Authors
- Palmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T.
- Affiliations
- La Trobe University (AU)
- The University of Queensland (AU)
- Corresponding author
- Ryan, Michael T.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 288
- Issue
- 38
- Pages
- 27584-27593
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3779755
- OpenAlex
- W2086718017
- Cited by
- 301
- References
- 61
- Citations by year
- 2026: 11 · 2025: 19 · 2024: 23 · 2023: 27 · 2022: 23 · 2021: 34 · 2020: 23 · 2019: 18 · 2018: 25 · 2017: 24 · 2016: 31 · 2015: 21 · 2014: 20 · 2013: 2
- FWCI
- 11.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- MiD51, Drp1, mitochondrial fission, Fis1, Mff, mitofusins, mitochondrial fusion, dominant negative effect
- MeSH terms
- Animals, HeLa Cells, Humans, Lysosomes, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Peptide Elongation Factors, Mice, Knockout, GTP Phosphohydrolases, Peroxisomes, Mitochondrial Proteins, Dynamins, Mice, Mitochondrial Dynamics
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