| Автор | Hinshaw, J. E. |
| Дата выпуска | 2000 |
| dc.description | ▪ 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. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | DYNAMIN AND ITS ROLE IN MEMBRANE FISSION <sup>1</sup> |
| DOI | 10.1146/annurev.cellbio.16.1.483 |
| Print ISSN | 1081-0706 |
| Журнал | Annual Review of Cell and Developmental Biology |
| Том | 16 |
| Первая страница | 483 |
| Последняя страница | 519 |
| Аффилиация | Hinshaw, J. E.; Laboratory of Cell Biochemistry and Biology, National Institutes of Health, Bethesda, Maryland 20892; e-mail: jennyh@helix.nih.gov |
