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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Increased cell surface expression and enhanced folding in the endoplasmic reticulum of a mutant erythropoietin receptor.
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Increased cell surface expression and enhanced folding in the endoplasmic reticulum of a mutant erythropoietin receptor.

机译：突变型促红细胞生成素受体的内质网中细胞表面表达的增加和折叠的增强。

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摘要

In both transfected and normal hematopoietic cells, the majority of newly made erythropoietin receptor (EPO-R) subunits are retained in the endoplasmic reticulum (ER), destined for degradation. Only a small fraction exit the ER and are competent to bind EPO, suggesting that the EPO-R folds inefficiently. The EPO-R contains a 5-amino acid motif, WSXWS, in the extracellular domain that is conserved among members of the cytokine receptor family. We describe a mutant EPO-R with a change in the middle residue of this motif, A234E, that is transported from the ER more efficiently than the wild-type (wt) receptor and is expressed in elevated numbers at the cell surface. This mutant polypeptide is processed more efficiently in the ER than its wt counterpart, suggesting that it folds better than the wt EPO-R. Inefficient folding and processing of the wt EPO-R in the ER may be one mechanism for controlling the number of plasma membrane receptors.
机译：在转染的和正常的造血细胞中，大多数新生成的促红细胞生成素受体（EPO-R）亚基都保留在内质网（ER）中，注定要降解。只有一小部分离开内质网并能结合EPO，这表明EPO-R折叠效率低下。 EPO-R在细胞外受体家族的成员中保守的细胞外结构域中包含5-氨基酸基序WSXWS。我们描述了一个突变的EPO-R，该基序的中间残基A234E发生了变化，它比野生型（wt）受体更有效地从ER转运，并在细胞表面以升高的数量表达。该突变体多肽在ER中比其wt对应物更有效地加工，表明它的折叠性比wt EPO-R好。 wt EPO-R在ER中的折叠效率低下和加工可能是控制质膜受体数量的一种机制。

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