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首页> 外文会议>International Congress on Genes, Gene Families and Isozymes >How Does the Cell Sense the Accumulation of Unfolded Proteins in the Endoplasmic Reticulum?
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How Does the Cell Sense the Accumulation of Unfolded Proteins in the Endoplasmic Reticulum?

机译：细胞如何感测成内质网中展开蛋白质的积累？

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摘要

The endoplasmic reticulum (ER)-located type Ⅰ transmembrane protein Ire1 is a key molecule for the unfolded protein response (UPR). Irel is dimerized and activated in response to ER stress. To understand the stress-sensing mechanism by Ire1, we performed a serial mutagenesis study of yeast Ire1 lumenal domain. The results predict that the Ire1 lumenal domain is divided into five subregions, among which subregions Ⅱ and Ⅳ are indispensable for Ire1 activity. Surprisingly the BiP-binding site was assigned to subregion Ⅴ, which is dispensable for UPR. We conclude that in the ER stress-sensory system, BiP is not the principal determinant of Ire1 activity, but an adjustor for sensitivity to various stresses, and that the predicted function of the core stress-sensing region (Ⅱ -Ⅳ) is to promote dimerization of Ire1 and BiP release from subregion Ⅴ.
机译：内质网（ER） - 均Ⅰ型跨膜蛋白IRE1是展开蛋白质反应（UPR）的关键分子。冰柱响应于ER应力而定化并激活。为了了解IRE1的应激感测机制，我们进行了酵母IRe1腔域的连续诱变研究。结果预测，IS1腔结构域分为五个亚区，其中Ⅱ次和Ⅳ次是IRE1活性不可或缺的。令人惊讶的是，将BIP结合位点分配给upr，其可分配给UPR。我们得出结论，在ER应激感觉系统中，BIP不是IS1活性的主要决定因子，而是一种针对各种应力的敏感性的调节器，并且核心应激感测区域的预测功能是促进从子区域ⅴ的IS1和BIP释放的二聚化。

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