DiAntonio Aaron, Hicke Linda
Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Annu Rev Neurosci. 2004;27:223-46. doi: 10.1146/annurev.neuro.27.070203.144317.
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.
通过泛素的共价连接对细胞蛋白质进行的翻译后修饰，可调节蛋白质的稳定性、活性和定位。泛素化快速且可逆，是对蛋白质活性进行空间和时间控制的有效机制。通过塑造突触的分子组成，这种多功能的翻译后修饰塑造了突触连接的模式、活性和可塑性。通过遗传、生化和电生理分析，正在确定受泛素化调节的突触过程，以及突触处的泛素化酶及其靶点。这项工作提供了诱人的线索，表明神经元活动与泛素化途径协同作用，以调节突触的结构和功能。
