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Published on: January 11, 2017
Mechanistic analysis of a dynamin effector.
Laura L Lackner1, Jennifer S Horner, Jodi Nunnari
1Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.
Science (New York, N.Y.)
|August 15, 2009
Summary
Dynamin-related proteins (DRPs) remodel membranes with help from DRP-associated proteins (DAPs). Mdv1, a DAP, aids mitochondrial division by promoting DRP assembly into force-generating helical structures.
Area of Science:
- Cell biology
- Molecular and cell biology
- Biochemistry
Background:
- Dynamin-related proteins (DRPs) are essential for membrane remodeling and cellular division.
- DRPs function in conjunction with DRP-associated proteins (DAPs) to carry out their cellular roles.
- The yeast mitochondrial division machinery, involving DRP Dnm1, Mdv1, and Fis1, serves as a model system.
Purpose of the Study:
- To elucidate the mechanistic role of a DRP-associated protein (DAP) in membrane remodeling.
- To understand how Mdv1 contributes to the function of the DRP Dnm1 in mitochondrial division.
Main Methods:
- Utilized the yeast mitochondrial division machine as a model system.
- Investigated the interaction and coassembly of Mdv1 with Dnm1.
- Analyzed the role of Mdv1 in regulating Dnm1 self-assembly into helical structures.
Main Results:
- Mdv1 acts post-mitochondrial targeting, specifically interacting with the GTP-bound form of Dnm1.
- This interaction nucleates and promotes the self-assembly of Dnm1 into helical structures.
- These helical Dnm1 structures are responsible for driving membrane scission during mitochondrial division.
Conclusions:
- Mdv1 plays a crucial role in regulating DRP assembly and function during mitochondrial division.
- The nucleation of DRP assembly by DAPs like Mdv1 is likely a general regulatory mechanism for filament-forming proteins.
- This mechanism is comparable to the regulation observed in F-actin assembly.
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