Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2

Sylvia Neumann, Sandra L. Schmid

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Background: Membrane curvature generation is essential for dynamin-2-catalyzed membrane fission and vesicle release. Results: Dynamin-2 binding partners with curvature generating activity differentially regulate the assembly, GTPase, and fission activities of dynamin-2. Conclusion: Dynamin-2 partners display complex patterns of regulation. Significance: The distinct functional interactions between dynamin-2 and its binding partners position them to contribute to the spatio-temporal regulation of clathrin-mediated endocytosis.

Original languageEnglish (US)
Pages (from-to)25119-25128
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number35
DOIs
StatePublished - Aug 30 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2'. Together they form a unique fingerprint.

Cite this