Assays and functional properties of auxilin-dynamin interactions

Sanja Sever, Jesse Skoch, Brian J. Bacskai, Sherri L. Newmyer

Research output: Contribution to journalReview articlepeer-review


The large GTPase dynamin is required for budding of clathrin-coated vesicles from the plasma membrane, but its mechanism of action is still not understood. Growing evidence indicates that the GTP-bound form of dynamin recruits downstream partners that execute the fission reaction. Recently, we reported nucleotide-dependent interactions between dynamin and auxilin, which suggested that auxilin cooperates with dynamin during vesicle formation. Here we describe three different in vitro assays that monitor auxilin-dynamin interactions, as well as fluorescence lifetime imaging microscopy that identify direct interactions between dynamin and auxilin in cells.

Original languageEnglish (US)
Article number50
Pages (from-to)570-585
Number of pages16
JournalMethods in enzymology
StatePublished - 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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