Intrapolypeptide interactions between the GTPase effector domain (GED) and the GTPase domain form the bundle signaling element in dynamin dimers.

Saipraveen Srinivasan, Juha Pekka Mattila, Sandra L. Schmid

Research output: Contribution to journalArticle

3 Scopus citations


Biochemical and structural studies of dynamin have shown that the C-terminus of the GTPase effector domain (GED) folds back and docks onto a platform created by the N- and C-terminal α-helices of the GTPase domain to form a three-helix bundle. While cross-linking studies suggested that insect cell-expressed dynamin existed as a domain-swapped dimer, X-ray structures of protein expressed in Escherichia coli failed to detect evidence of this domain swap. Here, by cross-linking several cysteine pair replacements and analyzing cross-linked species by matrix-assisted laser desorption ionization Mega time of flight, we conclude that dynamin is not domain-swapped and that GED-GTPase domain interactions occur in cis.

Original languageEnglish (US)
Pages (from-to)5724-5726
Number of pages3
Issue number36
Publication statusPublished - 2014


ASJC Scopus subject areas

  • Biochemistry

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