DOI: 10.1146/annurev.cellbio.16.1.483. Dynamin and Its Role in Membrane Fission

Dynamin and Its Role in Membrane Fission

10.1146/annurev.cellbio.16.1.483

Crossref journal-article

Annual Reviews

Annual Review of Cell and Developmental Biology (22)

Abstract

▪ Abstract Dynamin, a 100-kDa GTPase, is an essential component of vesicle formation in receptor-mediated endocytosis, synaptic vesicle recycling, caveolae internalization, and possibly vesicle trafficking in and out of the Golgi. In addition to the GTPase domain, dynamin also contains a pleckstrin homology domain (PH) implicated in membrane binding, a GTPase effector domain (GED) shown to be essential for self-assembly and stimulated GTPase activity, and a C-terminal proline-rich domain (PRD), which contains several SH3-binding sites. Dynamin partners bind to the PRD and may either stimulate dynamin's GTPase activity or target dynamin to the plasma membrane. Purified dynamin readily self-assembles into rings or spirals. This striking structural property supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission. The focus of this review is on the relationship between the GTPase and self-assembly properties of dynamin and its cellular function.

Bibliography

Hinshaw, J. E. (2000). Dynamin and Its Role in Membrane Fission. Annual Review of Cell and Developmental Biology, 16(1), 483â519.

Authors 1

J. E. Hinshaw (first)

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Dates

Type	When
Created	23 years, 1 month ago (July 27, 2002, 7:40 a.m.)
Deposited	2 years, 4 months ago (April 23, 2023, 2:16 p.m.)
Indexed	3 weeks, 6 days ago (Aug. 5, 2025, 8:23 a.m.)
Issued	24 years, 10 months ago (Nov. 1, 2000)
Published	24 years, 10 months ago (Nov. 1, 2000)
Published Print	24 years, 10 months ago (Nov. 1, 2000)

Funders 0

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BibTeX

@article{Hinshaw_2000, title={Dynamin and Its Role in Membrane Fission}, volume={16}, ISSN={1530-8995}, url={http://dx.doi.org/10.1146/annurev.cellbio.16.1.483}, DOI={10.1146/annurev.cellbio.16.1.483}, number={1}, journal={Annual Review of Cell and Developmental Biology}, publisher={Annual Reviews}, author={Hinshaw, J. E.}, year={2000}, month=nov, pages={483–519} }

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  "abstract": "<jats:p>\u25aa Abstract\u2002 Dynamin, a 100-kDa GTPase, is an essential component of vesicle formation in receptor-mediated endocytosis, synaptic vesicle recycling, caveolae internalization, and possibly vesicle trafficking in and out of the Golgi. In addition to the GTPase domain, dynamin also contains a pleckstrin homology domain (PH) implicated in membrane binding, a GTPase effector domain (GED) shown to be essential for self-assembly and stimulated GTPase activity, and a C-terminal proline-rich domain (PRD), which contains several SH3-binding sites. Dynamin partners bind to the PRD and may either stimulate dynamin's GTPase activity or target dynamin to the plasma membrane. Purified dynamin readily self-assembles into rings or spirals. This striking structural property supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission. The focus of this review is on the relationship between the GTPase and self-assembly properties of dynamin and its cellular function.</jats:p>",
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