Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095-1569, USA.
Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095-1569, USA
Development. 2020 Mar 18;147(6):dev175703. doi: 10.1242/dev.175703.
In essentially all eukaryotes, proteins can be modified by the attachment of small ubiquitin-related modifier (SUMO) proteins to lysine side chains to produce branched proteins. This process of 'SUMOylation' plays essential roles in plant and animal development by altering protein function in spatially and temporally controlled ways. In this Primer, we explain the process of SUMOylation and summarize how SUMOylation regulates a number of signal transduction pathways. Next, we discuss multiple roles of SUMOylation in the epigenetic control of transcription. In addition, we evaluate the role of SUMOylation in the etiology of neurodegenerative disorders, focusing on Parkinson's disease and cerebral ischemia. Finally, we discuss the possibility that SUMOylation may stimulate survival and neurogenesis of neuronal stem cells.
在几乎所有真核生物中，蛋白质可以通过将小泛素相关修饰物（SUMO）蛋白附着到赖氨酸侧链上来修饰，从而产生支链蛋白。这种“SUMO 化”过程通过以空间和时间控制的方式改变蛋白质功能，在动植物发育中起着至关重要的作用。在这篇综述中，我们解释了 SUMO 化的过程，并总结了 SUMO 化如何调节许多信号转导途径。接下来，我们讨论了 SUMO 化在转录的表观遗传控制中的多种作用。此外，我们评估了 SUMO 化在神经退行性疾病病因学中的作用，重点关注帕金森病和脑缺血。最后，我们讨论了 SUMO 化可能刺激神经元干细胞存活和神经发生的可能性。
