Wasik Urszula, Filipek Anna
Nencki Institute of Experimental Biology, Warsaw, Poland.
Nencki Institute of Experimental Biology, Warsaw, Poland.
Biochim Biophys Acta. 2014 Dec;1843(12):2878-2885. doi: 10.1016/j.bbamcr.2014.07.018. Epub 2014 Aug 7.
Post-translational modification by the SUMO moiety is now regarded as one of the key regulatory modifications in eukaryotic cells. Up to now, plenty of sumoylated proteins have been found to be involved in nuclear processes such as chromatin organization, transcription and DNA repair as well as in other cellular functions. Since the number of data concerning sumoylated proteins and their function outside the nucleus has grown rapidly, in this review we summarized the results describing the non-nuclear role of SUMO substrates. In particular, we focused on the role of sumoylation in the regulation of channel activity, receptor function, G-protein signaling, activity of enzymes, cytoskeletal organization, exocytosis, autophagy and mitochondrial dynamics.
小泛素样修饰物（SUMO）介导的翻译后修饰现在被认为是真核细胞中的关键调控修饰之一。到目前为止，已发现大量被SUMO化的蛋白质参与核过程，如染色质组织、转录和DNA修复以及其他细胞功能。由于关于被SUMO化的蛋白质及其在细胞核外功能的数据数量迅速增加，在本综述中，我们总结了描述SUMO底物非核作用的研究结果。特别地，我们重点关注了SUMO化在通道活性调节、受体功能、G蛋白信号传导、酶活性、细胞骨架组织、胞吐作用、自噬和线粒体动力学中的作用。
