Correlation between self-association modes and GTPase activation of dynamin

Derk D. Binns, Barbara Barylko, Nikolai Grichine, Mark A L Atkinson, Michael K. Helms, David M. Jameson, John F. Eccleston, Joseph P. Albanesi

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


The GTPase activity of dynamin is obligatorily coupled, by a mechanism yet unknown, to the internalization of clathrin-coated endocytic vesicles. Dynamin oligomerizes in vitro and in vivo and both its mechanical and enzymatic activities appear to be mediated by this self-assembly. In this study we demonstrate that dynamin is characterized by a tetramer/monomer equilibrium with an equilibrium constant of 1.67 x 1017 M-3. Stopped- flow fluorescence experiments Show that the association rate constant for 2'(Y)-O-N-methylanthraniloyl (mant)GTP is 7.0 x 10-5 M-1 s-1 and the dissociation rate constant is 2.1 s-1, whereas the dissociation rate constant for mantdeoxy GDP is 93 s-1. We also demonstrate the cooperativity of dynamin binding and GTPase activation on a microtubule lattice. Our results indicate that dynamin self-association is not a sufficient condition for the expression of maximal GTPase activity, which suggests that dynamin molecules must be in the proper conformation or orientation if they are to form an active oligomer.

Original languageEnglish (US)
Pages (from-to)277-290
Number of pages14
JournalJournal of Protein Chemistry
Issue number3
StatePublished - Jul 5 1999


  • Dynamin
  • GTPase activity
  • Self-association
  • Stopped-flow
  • mantGTP

ASJC Scopus subject areas

  • Biochemistry


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