Analysis of the ubiquitin-ligase complex in the endoplasmic reticulum membrane that regulates endoplasmic reticulum-associated degradation in mammals

内质网是合成多种蛋白质的细胞器。未能获得其天然构象的新合成的蛋白质被逆易位出ER，并在加入u B i qu i in s B后通过u B i qu i in s e c o m p l e s e s在ER膜中被降解。在本研究中，我们分析了复合物中各组分的稳定性，发现复合物组分的动态变化导致了错误折叠底物的降解。

Endoplasmic reticulum (ER) is an organelle in which v a r i o u s kinds of proteins are synthesized. Newly synthesized proteins that failed to obtain their native conformations are retrotranslocated out of the ER, and degraded by the cytoplasmic proteasome after the addition of u b i q u i t i n s b y t h e u b i q u i t i n l i g a s e c o m p l e x t h a t r e s i d e s in the ER membrane. In the present study, we have analyzed the stability of each component of the complex and found that the dynamic change of the component o f t h e c o m p l e x r e g u l a t e s the degradation of misfolded substrates.