An Intramolecular Signaling Element that Modulates Dynamin Function In Vitro and In Vivo
Mice, Knockout
Models, Molecular
0301 basic medicine
Binding Sites
Hydrolysis
Molecular Sequence Data
Clathrin-Coated Vesicles
Fibroblasts
Endocytosis
Cell Line
Dynamin II
Mice
Microscopy, Electron
03 medical and health sciences
Animals
Humans
Amino Acid Sequence
Guanosine Triphosphate
Fluorescent Antibody Technique, Indirect
Cells, Cultured
Dynamin I
Protein Binding
DOI:
10.1091/mbc.e09-04-0318
Publication Date:
2009-06-11T01:29:00Z
AUTHORS (6)
ABSTRACT
Dynamin exhibits a high basal rate of GTP hydrolysis that is enhanced by self-assembly on lipid template. Dynamin's GTPase effector domain (GED) required for this stimulation, though its mechanism action poorly understood. Recent structural work has suggested GED may physically dock with the to exert stimulatory effects. To examine how these interactions activate dynamin, we engineered minimal GTPase-GED fusion protein (GG) reconstitutes dynamin's activity and utilized it define framework mediates GED's association domain. Chemical cross-linking GG mutagenesis full-length dynamin establishes interface comprised N- C-terminal helices C-terminus GED. We further show essential stability in dynamin. Finally, identify mutations disrupt assembly-stimulated dynamin-catalyzed membrane fission vitro impair late stages clathrin-mediated endocytosis vivo. These data suggest components act as an intramolecular signaling module, which term bundle element, can modulate function
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CITATIONS (74)
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