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Updated: Jun 2, 2026

Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells
Published on: November 14, 2025
MiD49 and MiD51, new components of the mitochondrial fission machinery
Catherine S Palmer1, Laura D Osellame, David Laine
1La Trobe Institute for Molecular Science, La Trobe University, Plenty Road, Melbourne 3086, Victoria, Australia.
Abstract:
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.
Insights
New mitochondrial proteins, MiD49 and MiD51, regulate mitochondrial division by controlling the action of dynamin-related protein 1 (Drp1). Their presence is crucial for proper mitochondrial fission and network dynamics.
Area of Science:
- Cell Biology
- Mitochondrial Dynamics
- Protein Function
Background:
- Mitochondria exist as dynamic networks, constantly undergoing fission and fusion.
- Mitochondrial fission is mediated by proteins like dynamin-related protein 1 (Drp1).
Purpose of the Study:
- To identify novel proteins involved in mitochondrial fission.
- To elucidate the mechanism by which MiD49 and MiD51 regulate mitochondrial division.
Main Methods:
- Identification of mitochondrial outer membrane proteins MiD49 and MiD51.
- Analysis of MiD49/51 localization and interaction with Drp1.
- Knockdown and overexpression studies to assess functional impact.
Main Results:
- MiD49/51 form foci and rings on the mitochondrial outer membrane.
- MiD49/51 directly recruit Drp1 to mitochondria, promoting fission.
- Reduced MiD49/51 levels result in increased mitochondrial fusion.
- Overexpression of MiD49/51 leads to Drp1 sequestration and altered mitochondrial morphology.
Conclusions:
- MiD49 and MiD51 are novel mediators of mitochondrial division.
- MiD49/51 play a key role in regulating Drp1 activity at the mitochondria.
- These proteins are critical for maintaining mitochondrial network homeostasis.
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