title: Intrapolypeptide interactions between the GTPase effector domain (GED) and the GTPase domain form the bundle signaling element in dynamin dimers.
abstract: 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.
authors.affiliation: Department of Cell Biology, University of Texas Southwestern Medical Center , 5323 Harry Hines Boulevard, Dallas, Texas 75390, United States.
authors.forename: Saipraveen
authors.initials: S
authors.lastname: Srinivasan
authors.forename: Juha-Pekka
authors.initials: JP
authors.lastname: Mattila
authors.forename: Sandra L
authors.initials: SL
authors.lastname: Schmid
mesh_terms: D019281:Dimerization; D034281:Dynamins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D020558:GTP Phosphohydrolases; D034281:Dynamins