Abstract
The dynamin superfamily comprises a growing assortment of multi-domain GTPases, found from bacteria to man, that are distinguished from typical GTPases of the Ras, Rab and G-protein families by their modular structure (Figure 1), relatively large size (>70 kDa), and low affinity for guanine nucleotides. In addition, they display a conserved propensity to self-assemble into polymeric arrays, the dynamics of which are regulated by an autonomous, assembly-stimulated GTPase activity. Here, Ramachandran and Schmid describe the structural, biophysical, and biochemical properties of the dynamin superfamily and the implications for their distinct cellular functions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | R411-R416 |
| Journal | Current Biology |
| Volume | 28 |
| Issue number | 8 |
| DOIs | |
| State | Published - Apr 23 2018 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
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Ramachandran, R., & Schmid, S. L. (2018). The dynamin superfamily. Current Biology, 28(8), R411-R416. https://doi.org/10.1016/j.cub.2017.12.013