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

Sylvia Neumann; Sandra L. Schmid

doi:10.1074/jbc.M113.490474

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

Sylvia Neumann, Sandra L. Schmid

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

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.

Original language	English (US)
Pages (from-to)	25119-25128
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	35
DOIs	https://doi.org/10.1074/jbc.M113.490474
State	Published - Aug 30 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Schmid, Sandra L.

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N2 - 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.

AB - 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.

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

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