Dynamin rings: Not just for fission

Sanja Sever, Joann Chang, Changkyu Gu

Research output: Contribution to journalReview articlepeer-review

41 Scopus citations

Abstract

The GTPase dynamin has captivated researchers for over two decades, even managing to establish its own research field. Dynamin's allure is partly due to its unusual biochemical properties as well as its essential role in multiple cellular processes, which include the regulation of clathrin-mediated endocytosis and of actin cytoskeleton. On the basis of the classic model, dynamin oligomerization into higher order oligomers such as rings and helices directly executes the final fission reaction in endocytosis, which results in the generation of clathrin-coated vesicles. Dynamin's role in the regulation of actin cytoskeleton is mostly explained by its interactions with a number of actin-binding and -regulating proteins; however, the molecular mechanism of dynamin's action continues to elude us. Recent insights into the mechanism and role of dynamin oligomerization in the regulation of actin polymerization point to a novel role for dynamin oligomerization in the cell.

Original languageEnglish (US)
Pages (from-to)1194-1199
Number of pages6
JournalTraffic
Volume14
Issue number12
DOIs
StatePublished - Dec 2013
Externally publishedYes

Keywords

  • Dynamin actin
  • Endocytosis
  • Microtubules
  • Oligomerization

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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