The dynamin superfamily

Rajesh Ramachandran, Sandra L. Schmid

Research output: Contribution to journalShort survey

16 Scopus citations

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 languageEnglish (US)
Pages (from-to)R411-R416
JournalCurrent Biology
Volume28
Issue number8
DOIs
StatePublished - 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