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首页> 外文期刊>Journal of Cell Science >THE UNIQUE PROLINE-RICH DOMAIN OF PAROTID PROLINE-RICH PROTEINS FUNCTIONS IN SECRETORY SORTING
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THE UNIQUE PROLINE-RICH DOMAIN OF PAROTID PROLINE-RICH PROTEINS FUNCTIONS IN SECRETORY SORTING

机译：秘密排序中腮腺富含脯氨酸蛋白功能的唯一富含脯氨酸域

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When expressed in pituitary AtT-20 cells, parotid proline-rich proteins enter the regulated pathway. Because the short N-terminal domain of a basic proline-rich protein is necessary for efficient export from the ER, it has not been possible to evaluate the role of this polypeptide segment as a sorting signal for regulated secretion3. We now show that addition of the six-amino acid propeptide of proparathyroid hormone to the proline-rich protein, and especially to a deletion mutant lacking the N-terminal domain, dramatically accelerates intracellular transport of these polypeptides. Under these conditions the chimeric deletion mutant is stored as effectively as the full-length protein in dense core granules. The propeptide does not function as a sorting signal in AtT-20 cells as it does not reroute a constitutively secreted reporter protein to the regulated pathway. During transit, the propeptide is cleaved from the chimeric polypeptides such that the original structures of the full-length and the deletion mutant proline-rich proteins are reestablished. We have also found that the percentage stimulated secretion of the proline-rich proteins increases incrementally (almost twofold) as their level of expression is elevated. The increase reflects an enrichment of these polypeptides in the granule pool and its incremental nature suggests that sorting of proline-rich proteins involves an aggregation-based process. Because we can now rule out contributions to sorting by both N- and C-terminal segments of the proline-rich protein, we deduce that the unique proline-rich domain is responsible for storage. Thus at least some of the determinants of sorting for regulated secretion are protein-specific rather than universal. [References: 41]
机译：当在垂体AtT-20细胞中表达时，腮腺富含脯氨酸的蛋白质会进入调控途径。由于富含脯氨酸的基本蛋白质的短N端结构域对于从ER有效输出是必需的，因此尚不可能评估此多肽片段作为调节分泌的分类信号的作用。我们现在显示，脯氨酸丰富的蛋白质，特别是缺少N末端结构域的缺失突变体中，添加了甲状旁腺激素的6个氨基酸的前肽，可显着加速这些多肽的细胞内转运。在这些条件下，嵌合缺失突变体与全长蛋白质一样有效地存储在致密核心颗粒中。该前肽在AtT-20细胞中不充当分类信号，因为它不会将组成性分泌的报告蛋白重新引导至调节的途径。在转运过程中，将原肽从嵌合多肽上切割下来，从而重建全长和缺失突变型富含脯氨酸的蛋白质的原始结构。我们还发现随着脯氨酸表达水平的提高，富含脯氨酸的蛋白质的刺激分泌百分比逐渐增加（几乎两倍）。增加反映了这些多肽在颗粒池中的富集，其增量性质表明富含脯氨酸的蛋白质的分选涉及基于聚集的过程。因为我们现在可以排除对富含脯氨酸的蛋白质的N端和C端片段进行分类的贡献，所以我们推断出独特的富含脯氨酸的域负责存储。因此，至少有一些决定调节分泌的决定因素是蛋白质特异性的而不是普遍的。 [参考：41]

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