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- W1013077402 abstract "Dynamin, best studied for its role in clathrin-mediated endocytosis, is the prototypical member of a family of multi-domain GTPases involved in fission and remodeling of multiple organelles. Dynamin alone can catalyze fission of membrane tubules and vesicle formation from planar lipid templates. We recently proposed a two-stage model for dynamin-catalyzed fission (Frolov and Schmid, Ann. Rev. Cell and Dev. Biol. 2011. 27: 79). In stage one, mechanochemical activities of assembled dynamin helices induce localized curvature stress. In stage two the tightly packed lipid-interacting pleckstrin homology domains insert hydrophobic wedges into the bilayer to create a catalytic center that guides lipid remodeling and drives membrane fission through hemi-fission intermediates. We have been using site-directed fluorescent labeling of dynamin to the study nucleotide-dependent conformational changes required for dynamin-catalyzed fission. Our data suggests that a concerted conformational change and coordinated GTP hydrolysis are required for dynamin-catalyzed fission. We are also studying the role of BAR domain-containing proteins as dynamin partners in membrane fission." @default.
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- W1013077402 date "2013-04-01" @default.
- W1013077402 modified "2023-09-23" @default.
- W1013077402 title "Mechanism of Dynamin‐Catalyzed Membrane Fission" @default.
- W1013077402 doi "https://doi.org/10.1096/fasebj.27.1_supplement.212.1" @default.
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