RING结构泛素连接酶RNF186的功能研究
摘要
内质网中错误折叠蛋白的积累以及Ca2+平衡的紊乱会引起一系列决定细胞存活还是死亡的信号反应。泛素化系统是这一系列反应中重要的调控因素,E3泛素连接酶为泛素化系统提供了反应特异性,而RING结构蛋白E3连接酶是泛素连接酶中数量最多的一大类,它们在维持基因组的稳定性以及正常的细胞生理活动过程中发挥了重要的调节作用。人类新基因RNG186(RING Finger Protein186)是一个典型的C3HC4型RING结构蛋白,广泛表达于哺乳动物的各种组织、常见的细胞系中。RNF186基因结构较高的保守性提示其可能在基本的生物学功能方面发挥着重要的作用,本论文在分子细胞水平上对RNF186的生物学功能作了初步的探索。我们发现：外源性RNF186能引起ER stress关键性调控蛋白的上调；并能促使ER中Ca2+释放到细胞基质中。而内源性敲低RNF186的表达则对ER stress诱导剂thapsigargin所引起的UPR反应有一定的抑制。这表明RNF186在ER stress途径的细胞凋亡通路中可能发挥重要作用。我们进一步鉴定出Bcl-2家族的蛋白BNip1是RNF186的泛素化底物,RNF186通过对它进行泛素的第29位和63位赖氨酸的多聚泛素化修饰,促进其转位到线粒体上,但不改变其蛋白水平。内源性敲低BNip1对RNF186引起的ER stress现象有明显的抑制,而在thapsigargin诱导下,BNip1的泛素化现象增强,这伴随着RNF186的蛋白稳定性增强。这些结果表明,BNip1可能是一个位于RNF186下游的调控蛋白,随着ER stress的发生,RNF186稳定性增强,通过对BNip1的泛素化,促使其一方面在ER上发挥放大ER strss信号的下游调控作用,另一方面转移到线粒体,可能会参与线粒体途径的凋亡调控。我们的研究揭示了RING结构E3连接酶参与ER stress凋亡调控的新机制,并为疾病的治疗开启了一个新的思路。
The ubiquitination of proteins plays an important role in regulating many cellular and organismal processes. Ub conjugation to the target protein via an isopeptide bound between its C-terminal glycine and the lysine residue of the substrate involves a cascade of enzymatic reactions. E3ligases play central regulatory roles in the ubiquitination cascade reactions. There are two major types of E3ligases in eukaryotic cells:HECT E3s and ringer finger E3s defined by the presence of their specific E2recruiting domains. RING finger E3s are the most numerous and about616members have been discovered in human cells up to now.
ER is a very important organelle involved in many essential cellular processes which are required for cell survival. Most importantly of these processes are protein modification, sorting and transportation. In eukaryotic cells, proteins enter the ER as unfolded polypeptide, only after they snap into the right conformation,these secreted and transmembrane proteins can be transported to the destination. Cells have evolved a precise system to adjust the protein-folding capacity in order to adapt different environment stress. Such strict regulation is achieved through intracellular signaling pathway which named unfolded protein response(UPR). Disturbance in the ER calcium regulation is one of the stress signals because the high calcium concentration in the ER is necessary for protein folding. Bcl-2family on guard at the ER can regulate the release of calcium into the cytosol from ER.
BNip proteins are a pro-apoptotic subgroup of Bcl-2family, which have a conserved BH3domain. The BNip group of proteins include BNipl, BNip2, BNip3and Nix in humans. BNipl is a228amino acid protein and has a carboxyl terminal transmembrane (TM) domain which enable it to localize in ER. Some previous papers reported that BNip1played a role in induction of apoptosis, maintaining the integrity of the ER network and mitochondrial fragmentation. Here we demonstrate that one ring finger E3RNF186plays a important role in regulating ER stress associated apoptosis by interacting with BNipl.
The ubiquitination of proteins plays an important role in regulating many cellular and organismal processes. Ub conjugation to the target protein via an isopeptide bound between its C-terminal glycine and the lysine residue of the substrate involves a cascade of enzymatic reactions. E3ligases play central regulatory roles in the ubiquitination cascade reactions. There are two major types of E3ligases in eukaryotic cells:HECT E3s and ringer finger E3s defined by the presence of their specific E2recruiting domains. RING finger E3s are the most numerous and about616members have been discovered in human cells up to now.
ER is a very important organelle involved in many essential cellular processes which are required for cell survival. Most importantly of these processes are protein modification, sorting and transportation. In eukaryotic cells, proteins enter the ER as unfolded polypeptide, only after they snap into the right conformation,these secreted and transmembrane proteins can be transported to the destination. Cells have evolved a precise system to adjust the protein-folding capacity in order to adapt different environment stress. Such strict regulation is achieved through intracellular signaling pathway which named unfolded protein response(UPR). Disturbance in the ER calcium regulation is one of the stress signals because the high calcium concentration in the ER is necessary for protein folding. Bcl-2family on guard at the ER can regulate the release of calcium into the cytosol from ER.
BNip proteins are a pro-apoptotic subgroup of Bcl-2family, which have a conserved BH3domain. The BNip group of proteins include BNipl, BNip2, BNip3and Nix in humans. BNipl is a228amino acid protein and has a carboxyl terminal transmembrane (TM) domain which enable it to localize in ER. Some previous papers reported that BNip1played a role in induction of apoptosis, maintaining the integrity of the ER network and mitochondrial fragmentation. Here we demonstrate that one ring finger E3RNF186plays a important role in regulating ER stress associated apoptosis by interacting with BNipl.
引文
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