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DRP1 and MID49 co-diffusion scans mitochondria for fission
Cristiana Zollo1,2, David Gomez Suarez2,3, Elmira Parvindokht Bararpour1,2
1Institute of Genetics, University of Cologne, Cologne, Germany.
Abstract:
DRP1 is a dynamin-related large GTPase responsible for mitochondrial fission, which ensures proper mitochondrial distribution, morphology and quality control. Despite its relevance, the mechanism of mitochondrial division, especially regarding the dynamic regulation of DRP1, remains elusive. Here we report that DRP1 oligomers diffuse in helical-like trajectories along mitochondria, browsing the organelle surface and stalling at preconstricted fission sites, in what we call 'mito-scanner' motion. Molecular dynamics simulations support a geometry-mediated diffusion mechanism emerging from surface confinement. Perturbation of DRP1 motility results in elongated mitochondria, underscoring the functional importance of DRP1 scanning dynamics in mitochondrial division. We also show that DRP1 dynamics on mitochondria are differentially regulated by interactions with its adaptors, where co-diffusion of MID49/MID51 with DRP1 promotes its motility. Our findings support a model in which receptor-regulated mitochondrial surveillance by DRP1 enables balanced organelle division, with potential implications for targeting this process in disease.
Insights
Dynamin-related protein 1 (DRP1) moves along mitochondria like a scanner, a motion crucial for cell division. This "mito-scanner" behavior, regulated by adaptors, ensures healthy mitochondria and impacts disease.
Area of Science:
- Cell Biology
- Molecular Biology
- Biophysics
Background:
- Mitochondrial fission is vital for cellular health, regulated by dynamin-related protein 1 (DRP1).
- The precise mechanism and dynamic regulation of DRP1 during mitochondrial division remain unclear.
Purpose of the Study:
- To elucidate the dynamic behavior of DRP1 on mitochondria during fission.
- To understand how DRP1 motility is regulated and its functional significance.
Main Methods:
- Observation of DRP1 oligomer movement using advanced microscopy.
- Molecular dynamics simulations to model DRP1 diffusion.
- Perturbation studies to assess the impact of DRP1 motility changes.
Main Results:
- DRP1 oligomers exhibit a novel "mito-scanner" motion, diffusing helically along mitochondria and stalling at fission sites.
- Molecular dynamics simulations confirm a geometry-mediated diffusion mechanism.
- Disrupting DRP1 motility leads to elongated mitochondria, highlighting the importance of its scanning dynamics.
- Interactions with adaptors like MID49/MID51 differentially regulate DRP1 motility, with co-diffusion enhancing it.
Conclusions:
- DRP1's "mito-scanner" motion is a key mechanism for mitochondrial surveillance and division.
- Receptor-mediated regulation of DRP1 dynamics is essential for balanced mitochondrial division.
- Understanding DRP1 dynamics offers potential therapeutic targets for diseases involving mitochondrial dysfunction.
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