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Cited by 699

The DOI matches its Crossref record; 208 of the 208 references it cites were found in a registry or an index.

Dynamin and Its Role in Membrane Fission

Open access
Hinshaw, J. E.·2000·Annual Review of Cell and Developmental Biology

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.

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Metadata

Authors
Hinshaw, J. E.
Venue
Annual Review of Cell and Developmental Biology
Published
2000-11
Volume
16
Issue
1
Pages
483-519
ISSN
  • 1081-0706 (ISSN-L)
  • 1530-8995
OpenAlex
W2157920366
Cited by
699
References
208
FWCI
2.41
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Dynamin and Its Role in Membrane Fission. https://app.cochat.ai/papers/10.1146/annurev.cellbio.16.1.483
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Hinshaw, J. E. (2000). Dynamin and Its Role in Membrane Fission. Annual Review of Cell and Developmental Biology. https://doi.org/10.1146/annurev.cellbio.16.1.483

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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