Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
@article{Hinshaw1995DynaminSI, title={Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding}, author={Jenny E. Hinshaw and Sandra L. Schmid}, journal={Nature}, year={1995}, volume={374}, pages={190-192} }
DYNAMIN, a 100K member of the GTPase superfamily1, is the mammalian homologue of the Drosophila shibire gene product2,3. Mutations in shibire cause a defect in endocytosis leading to accumulation of coated pits and deep imaginations at the plasma membrane of all tissues examined4,5. Similarly, invaginated coated pits accumulate in mammalian cells overexpressing dominant-negative mutants of dynamin, establishing that dynamin is required for the formation of 'constricted' coated pits and for…
850 Citations
The Role of Dynamin and Its Binding Partners in Coated Pit Invagination and Scission
- Biology, ChemistryThe Journal of cell biology
- 2001
Dynamin is shown to be required for the late stages of invagination of clathrin-coated pits, and dynamin must bind and hydrolyze GTP for its role in sequestering ligand into deeply invaginated coated pits.
Dynamin Mediates Membrane Vesiculation
- BiologyMicroscopy and Microanalysis
- 1998
It is shown that purified recombinant dynamin can bind to a lipid bilayer in a regular and repeating pattern to form helical tubes which vesiculate upon the addition of GTP.
Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
- Biology, ChemistryNature
- 1995
These findings demonstrate that dynamin and clathrin act at different sites in the formation of endocytic vesicles and suggest that stabilization of the GTP-bound conformation of dynamin leads to tubule formation by progressive elongation of the vesicle stalk.
Dynamin:Gtp Controls the Formation of Constricted Coated Pits, the Rate Limiting Step in Clathrin-Mediated Endocytosis
- Biology, ChemistryThe Journal of cell biology
- 2000
Using stage-specific assays and morphological analyses of stably transformed cells, data support a model in which dynamin functions like a classical GTPase as a key regulator of clathrin-mediated endocytosis.
Dynamin and its role in membrane fission.
- Biology, ChemistryAnnual review of cell and developmental biology
- 2000
Purified dynamin readily self-assembles into rings or spirals, which supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission.
Physical and functional connection between auxilin and dynamin during endocytosis
- Chemistry, BiologyThe EMBO journal
- 2006
The model that the GTP‐bound conformation of dynamin tetramers stimulates formation of constricted coated pits at the plasma membrane by regulating the chaperone activity of hsc70/auxilin is supported.
Auxilin-dynamin interactions link the uncoating ATPase chaperone machinery with vesicle formation.
- BiologyDevelopmental cell
- 2003
Dynamin self-assembly and the vesicle scission mechanism: how dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis.
- Chemistry, BiologyBioEssays : news and reviews in molecular, cellular and developmental biology
- 2010
The new model of the dynamin oligomer has the potential to explain how short self-limiting fissogenic dynamin assemblies are formed and how concerted GTP hydrolysis is achieved.
Three-dimensional reconstruction of dynamin in the constricted state
- BiologyNature Cell Biology
- 2001
The structure suggests that the dense stalk and head regions rearrange when GTP is added, a rearrangement that generates a force on the underlying lipid bilayer and thereby leads to membrane constriction, indicating that dynamin is a force-generating 'contrictase'.
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