Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane.

ABSTRACT: The GTPase dynamin is a mechanochemical enzyme involved in membrane fission, but the molecular nature of its membrane interactions and their regulation by guanine nucleotides and protein effectors remain poorly characterized. Using site-directed fluorescence labeling and several independent fluorescence spectroscopic techniques, we have developed robust assays for the detection and real-time monitoring of dynamin-membrane and dynamin-dynamin interactions. We show that dynamin interacts preferentially with highly curved, PIP2-dense membranes and inserts partially into the lipid bilayer. Our kinetic measurements further reveal that cycles of GTP binding and hydrolysis elicit major conformational rearrangements in self-assembled dynamin that favor dynamin-membrane association and dissociation

SUBMITTER: Ramachandran R 

PROVIDER: S-EPMC2206142 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature