The dynamin superfamily: universal membrane tubulation and fission molecules?

@article{Praefcke2004TheDS,
  title={The dynamin superfamily: universal membrane tubulation and fission molecules?},
  author={Gerrit J. K. Praefcke and Harvey T. McMahon},
  journal={Nature Reviews Molecular Cell Biology},
  year={2004},
  volume={5},
  pages={133-147}
}
Dynamins are large GTPases that belong to a protein superfamily that, in eukaryotic cells, includes classical dynamins, dynamin-like proteins, OPA1, Mx proteins, mitofusins and guanylate-binding proteins/atlastins. They are involved in many processes including budding of transport vesicles, division of organelles, cytokinesis and pathogen resistance. With sequenced genomes from Homo sapiens, Drosophila melanogaster, Caenorhabditis elegans, yeast species and Arabidopsis thaliana, we now have a… 
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References

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TLDR
It is established that human MxA, despite sharing only 30% homology with conventional dynamin, possesses many of these properties, including the propensity to self-assemble, an affinity for lipids, and the ability to tubulate membranes.
GTPase activity of dynamin and resulting conformation change are essential for endocytosis
TLDR
It is shown that oligomerization and GTP binding alone, by dynamin, are not sufficient for endocytosis in vivo, and efficient GTP hydrolysis and an associated conformational change are also required.
Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
TLDR
It is reported that the primitive red alga Cyanidioschyzon merolae retains only one dynamin homolog, CmDnm1, belonging to the mitochondrial division subfamily, which is probably not required for early constriction; it forms a ring or spiral when the outer mitochondrial membrane is finally severed.
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TLDR
Evidence for the oligomeric state of dynamin at high and low ionic strength conditions is reviewed and the possible mechanism by which assembly of Dynamin leads to an increase in its GTPase activity is discussed.
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TLDR
It is proposed that mitochondrial fission in yeast is a multi-step process, and that membrane-bound Fis1p is required for the proper assembly, membrane distribution, and function of Dnm1p-containing complexes during fission.
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TLDR
The structure suggests that the dense stalk and head regions rearrange when GTP is added, a rearrangement that generates a force on the underlying lipid bilayer and thereby leads to membrane constriction, indicating that dynamin is a force-generating 'contrictase'.
The dynamin A ring complex: molecular organization and nucleotide‐dependent conformational changes
TLDR
Nucleotide‐dependent changes observed with the unmodified and modified protein support a mechanochemical action of dynamin, in which tightening and stretching of a helix contribute to membrane fission.
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