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  • Structure Watch
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Structure watch

Nature Reviews Molecular Cell Biology volume 12, page 623 (2011)Cite this article

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Dynamin-related proteins (DRPs) are multidomain GTPases that can regulate membrane remodelling events. Although DRPs are known to undergo oligomerization and GTP-dependent conformational changes, it is less clear how these properties drive membrane remodelling.

Ford et al. determined the crystal structure of a dynamin that is assembly deficient. They isolated a Gly397Asp mutation in rat dynamin 1 lacking its Pro-rich domain that strongly inhibits dynamin self-assembly. This allowed them to elucidate the crystal structure of dynamin 1 in a nucleotide-free state and revealed an extended structure, in which the GTPase domain and bundle signalling element (BSE) reside on top of a long helical stalk, with the pleckstrin homology (PH) domain positioned at the other end of the stalk. Faelber et al. similarly determined the crystal structure of human dynamin 1 in the nucleotide-free state by identifying mutations that disrupt oligomer formation. Further analysis by both groups characterized the role of the stalk region in mediating dimer and multimer formation.

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ORIGINAL RESEARCH PAPERS

  1. Ford, M. G. J., Jenni, S. & Nunnari, J. The crystal structure of dynamin. Nature 18 Sept 2011 (doi: 10.1038/nature10441)

    Article  CAS  Google Scholar 

  2. Faelber, K. et al. Crystal structure of nucleotide-free dynamin1. Nature 18 Sept 2011 (doi: 10.1038/nature10369)

    Article  CAS  Google Scholar 

  3. Chao, L. H. et al. A mechanism for tunable autoinhibition in the structure of a human Ca2+/calmodulin-dependent kinase II holoenzyme. Cell 146, 732–745 (2011) Article

    Article  CAS  Google Scholar 

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Structure watch. Nat Rev Mol Cell Biol 12, 623 (2011). https://doi.org/10.1038/nrm3203

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