Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2

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Abstract

Background: Membrane curvature generation is essential for dynamin-2-catalyzed membrane fission and vesicle release. Results: Dynamin-2 binding partners with curvature generating activity differentially regulate the assembly, GTPase, and fission activities of dynamin-2. Conclusion: Dynamin-2 partners display complex patterns of regulation. Significance: The distinct functional interactions between dynamin-2 and its binding partners position them to contribute to the spatio-temporal regulation of clathrin-mediated endocytosis. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Neumann, S., & Schmid, S. L. (2013). Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2. Journal of Biological Chemistry, 288(35), 25119–25128. https://doi.org/10.1074/jbc.M113.490474

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