SIN3A複合體於基因抑制表現中扮演重要的角色。它是利用組蛋白去乙烯酶1/2去除乙烯基而使得RNA合成酶無法集合上DNA轉錄出RNA達到基因表達抑制的效果。而SIN3A複合體的組成因子有RBBP4, RBBP7, SAP18, SAP180/ARID4B, SAP130, SAP25, SAP45與 SAP30/SAP30L。其中SAP130已被證明參與了SIN3A複合物的抑制基因表達作用。本實驗室在先前的研究中使用了酵母菌雜合實驗發現SAP130和Fas 受體結合蛋白FAF1有著蛋白質交互作用關係，並且發現SAP130可以被SUMO1修飾。另一方面， FAF1參與了多種的功能，像是調節細胞凋亡、蛋白質泛素化、NF-κB與Wnt/β-catenin路徑等，因此被認為是一個支架蛋白(scaffold protein)。在此研究中利用了SAP130 SUMO位點的突變體去了解SAP130的SUMO化在NF-κB 路徑與 Wnt/β-catenin路徑扮演什麼樣的角色。另外，本研究也使用酵母菌雙雜合系統(yeast two-hybrid screening)尋找是否還有其他能與SAP130進行交互作用的蛋白。在未來，本研究會繼續探討FAF1與Sin3A/SAP130複合體在細胞中扮演的角色。

SIN3A complex plays an important role in gene silencing. It uses histone deacetylase 1/2 enzymatic activity to remove acetyl group on histone and prohibits RNA polymerase to initiate the transcription to repress gene expression. Several SIN3A complex co-factors have been identified including SAP18, SAP25, SAP45, SAP30/SAP30L, SAP130, SAP180/ARID4B and Rbbp4/7. Among them, Sin3A associated protein 130 (SAP130) has been known to be one of the most important factors affecting SIN3A-mediated transrepression. In our previous study, we have identified SAP130 as a novel Fas-associated factor (FAF)-1 interacting protein. Furthermore, we found that SAP130 protein can be modified by SUMO1. FAF1 is a scaffold protein that have been known to be involved in numerous of biological processes including apoptosis, protein ubiquitination, Wnt/β-catenin and NF-κB signaling pathways. In this study, I have characterized the role of SUMO-modified SAP130 in NF-κB and Wnt/β-catenin signaling. In addition, I have identified several novel SAP130 interacting partners by yeast two-hybrid screening. Further study will clarify the interplay between FAF1 and Sin3A/SAP130 functions in
different cellular processes.

林弘偉，探討Sin3A結合蛋白(SAP130)類泛素化修飾之調節分析，國立
成功大學生物科技與產業科學系碩士論文，2018.

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