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首页> 美国卫生研究院文献>The EMBO Journal >The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
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The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum

机译：KDEL受体介导回收机制有助于内质网的质量控制

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摘要

Newly synthesized proteins in the endoplasmic reticulum (ER) must fold and assemble correctly before being transported to their final cellular destination. While some misfolded or partially assembled proteins have been shown to exit the ER, they fail to escape the early secretory system entirely, because they are retrieved from post-ER compartments to the ER. We elucidate a mechanistic basis for this retrieval and characterize its contribution to ER quality control by studying the fate of the unassembled T-cell antigen receptor (TCR) α chain. While the steady-state distribution of TCRα is in the ER, inhibition of retrograde transport by COPI induces the accumulation of TCRα in post-ER compartments, suggesting that TCRα is cycling between the ER and post-ER compartments. TCRα associates with BiP, a KDEL protein. Disruption of the ligand-binding function of the KDEL receptor releases TCRα from the early secretory system to the cell surface, so that TCRα is no longer subject to ER degradation. Thus, our findings suggest that retrieval by the KDEL receptor contributes to mechanisms by which the ER monitors newly synthesized proteins for their proper disposal.
机译：内质网（ER）中新合成的蛋白质必须折叠并正确组装，然后才能运输到它们的最终细胞目的地。虽然已经显示一些错误折叠或部分组装的蛋白质会离开ER，但它们无法完全逃脱早期分泌系统，因为它们是从ER后的隔室中回收到ER的。我们通过研究未组装的T细胞抗原受体（TCR）α链的命运，阐明了这种检索的机制基础，并表征了其对ER质量控制的贡献。 TCRα的稳态分布在ER中，而COPI抑制逆行转运会诱导TCRα在ER后腔室中积聚，这表明TCRα在ER和ER后腔室之间循环。 TCRα与KDEL蛋白BiP结合。破坏KDEL受体的配体结合功能会将TCRα从早期分泌系统释放到细胞表面，因此TCRα不再受ER降解的影响。因此，我们的发现表明，通过KDEL受体进行的检索有助于ER监测新合成蛋白质的正确处置机制。

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