| Автор | DiAntonio, Aaron |
| Автор | Hicke, Linda |
| Дата выпуска | 2004 |
| dc.description | ▪ Abstract Posttranslational modification of cellular proteins by the covalent attachment of ubiquitin regulates protein stability, activity, and localization. Ubiquitination is rapid and reversible and is a potent mechanism for the spatial and temporal control of protein activity. By sculpting the molecular composition of the synapse, this versatile posttranslational modification shapes the pattern, activity, and plasticity of synaptic connections. Synaptic processes regulated by ubiquitination, as well as ubiquitination enzymes and their targets at the synapse, are being identified by genetic, biochemical, and electrophysiological analyses. This work provides tantalizing hints that neuronal activity collaborates with ubiquitination pathways to regulate the structure and function of synapses. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE |
| DOI | 10.1146/annurev.neuro.27.070203.144317 |
| Print ISSN | 0147-006x |
| Журнал | Annual Review of Neuroscience |
| Том | 27 |
| Первая страница | 223 |
| Последняя страница | 246 |
| Аффилиация | DiAntonio, Aaron; Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110 email: diantonio@wustl.edu |
