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… 
The Role of Dynamin and Its Binding Partners in Coated Pit Invagination and Scission
TLDR
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
TLDR
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
TLDR
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
TLDR
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 A Molecular Motor with Pinchase Action
Dynamin and its role in membrane fission.
  • J. Hinshaw
  • Biology, Chemistry
    Annual review of cell and developmental biology
  • 2000
TLDR
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
TLDR
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.
Dynamin self-assembly and the vesicle scission mechanism: how dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis.
  • N. Pawlowski
  • Chemistry, Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2010
TLDR
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
TLDR
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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References

SHOWING 1-10 OF 13 REFERENCES
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
TLDR
It is concluded that dynamin is specifically required for endocytic coated vesicle formation, and that its GTP binding and hydrolysis activities are required to form constricted coated pits and, subsequently, for coatedvesicle budding.
Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
TLDR
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.
Mutations in human dynamin block an intermediate stage in coated vesicle formation
TLDR
Results demonstrate that mutations in the GTP-binding domain of dynamin block Tfn-endocytosis in mammalian cells and suggest that a functional dynamin GTPase is required for receptor-mediated endocytotic via clathrin-coated pits.
Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis
TLDR
Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting9,10.
Multiple GTP-binding proteins participate in clathrin-coated vesicle- mediated endocytosis
TLDR
It is demonstrated that multiple GTP-binding proteins, including heterotrimeric G proteins, participate at discrete stages in receptor- mediated endocytosis via clathrin-coated pits.
Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
TLDR
The shibire gene product and dynamin have extensive similarity, and it is suggested that these proteins provide the motor for vesicular transport during endocytosis and are cognate homologues.
Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain.
TLDR
The basic, proline-rich C-terminal region of dynamin is identified as the binding site for both microtubules and SH3 domains and an allosteric interaction between this region of the molecule and the N-terminals of the GTPase domain is demonstrated.
Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila.
TLDR
The temperature-sensitive Drosophila mutant, shibirets1 (shi), has been shown to exhibit a reversible block in synaptic transmission at 30 degrees C, and the accumulation of many pitlike structures on the plasma membrane near presynaptic sites are referred to as "collared pits".
Interaction of dynamin with microtubules: its structure and GTPase activity investigated by using highly purified dynamin.
TLDR
Despite slow GTPase turnover rate in the absence of microtubules, binding of GTP and its nonhydrolizing analogues was very fast, indicating that GTP binding step is not rate limiting.
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