Sumoylation regulates diverse biological processes.
Sumoylation regulates diverse biological processes.
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DOI：
10.1007/s00018-007-7137-4
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发表时间：
2007-12
期刊：
影响因子：
--
通讯作者：
Zhao J
中科院分区：
文献类型：
--
作者：
Zhao J
在发现十年后，这种类似泛素的小蛋白修饰物(SUMO)已经成为蛋白质的关键调节因子。虽然早期的研究表明，苏木酸化主要发生在细胞核内，但最近发现了越来越多的非核底物，这表明细胞中的苏木酸化阶段更广。与泛素化不同，泛素化主要针对底物进行降解，和素化主要通过改变细胞内定位、蛋白质-蛋白质相互作用或其他类型的翻译后修饰来调节底物的功能。这些变化反过来影响基因表达、基因组和染色体的稳定性和完整性，以及信号转导。和甲基化被脱氨甲基化抵消，而平衡的总甲基化对于正常的细胞行为是必不可少的。平衡的丧失与许多疾病有关。本文综述了相扑通路、底物和细胞功能的最新研究进展，重点介绍了一些重要的发现，这些发现加速了相扑研究领域的进展，并将相扑与人类疾病联系起来。
Ten years after its discovery, the small ubiquitin-like protein modifier (SUMO) has emerged as a key regulator of proteins. While early studies indicated that sumoylation takes place mainly in the nucleus, an increasing number of non-nuclear substrates have recently been identified, suggesting a wider stage for sumoylation in the cell. Unlike ubiquitylation, which primarily targets a substrate for degradation, sumoylation regulates a substrate’s functions mainly by altering the intracellular localization, protein-protein interactions or other types of post-translational modifications. These changes in turn affect gene expression, genomic and chromosomal stability and integrity, and signal transduction. Sumoylation is counter-balanced by desumoylation, and well-balanced sumoylation is essential for normal cellular behaviors. Loss of the balance has been associated with a number of diseases. This paper reviews recent progress in the study of SUMO pathways, substrates, and cellular functions and highlights important findings that have accelerated advances in this study field and link sumoylation to human diseases.
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