Pichler Andrea, Fatouros Chronis, Lee Heekyoung, Eisenhardt Nathalie
Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
Max Planck Institute of Immunobiology and Epigenetics, Department of Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
Biomol Concepts. 2017 Mar 1;8(1):13-36. doi: 10.1515/bmc-2016-0030.
The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate. We focus on the interplay of the E1, E2 and E3 enzymes and discuss how specificity could be achieved given the limited number of conjugating enzymes and the thousands of substrates.
通过与小泛素相关修饰物（SUMO）进行修饰来调节蛋白质命运，在大多数细胞途径中起着至关重要的作用。由于SUMO缀合和去缀合的相反作用，SUMO化具有高度动态性。SUMO缀合由E1、E2和E3酶的分级作用完成，而去缀合涉及SUMO特异性蛋白酶。在本综述中，我们总结并比较了SUMO与其底物缀合的机制原理。我们重点关注E1、E2和E3酶之间的相互作用，并讨论在缀合酶数量有限而底物有成千上万种的情况下如何实现特异性。
