波谱学杂志Issue(2)：163-180,18.DOI:10.11938/cjmr20150203
利用核磁共振法探讨类泛素媒介的信息传导分子机制
Probing the Molecular Basis of SUMO-Mediated Signaling Pathway by NMR
黄太煌1
作者信息
- 1. 生物医学利学研究所,台湾台北11529;基因体研究中心,台湾台北11529;台湾师范大学物理系,台湾台北11677
- 折叠
摘要
Abstract
Post-translational modification by Small Ubiquitin-like MOdifier (SUMO) proteins regulates a diverse array of cellular events. The signaling process is initiated by attaching SUMO to the E1 activating protein. In the second step SUMO is transferred to E2 conjugating protein (Ubc9). Lastly, Ubc9 couples SUMO to a target substrate covalently. The process is terminated by protease removal of SUMOs from the substrates. Sumoylation is regulated primarily through specific recognition of the sumoylation motif (SM) by Ubc9 and, in some cases, by E3-substrate recognition. The functional consequences of SUMO modification are mostly mediated by recruitment of effector proteins that contain a SUMO Interaction Motif (SIM). Furthermore, SUMO can form poly-SUMO conjugate, which can be recognized by proteins containing poly-SIMs, such as the RING-finger 4 (RNF4) ubiquitin E3 ligase. RNF4 contains four SIMs that facilitate poly-SUMO-specific ubiquitination and targets poly-sumoylated proteins for degradation. Here we review NMR structure-functional studies, conducted in our laboratory and aimed at dissecting the molecular basis of SUMO-mediated pathway.关键词
液体核磁共振/结构/类泛素/急性前髓细胞白血蛋白/Daxx/RNF4Key words
liquid NMR/structure/SUMO/PML/Daxx/RNF4分类
数理科学引用本文复制引用
黄太煌..利用核磁共振法探讨类泛素媒介的信息传导分子机制[J].波谱学杂志,2015,(2):163-180,18.
