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首页> 外文期刊>EMBO Journal >A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.
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A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.

机译:一种新颖的胞质类抗原加工途径为endoplasmic-reticulum-targeted蛋白质。

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摘要

Proteins bearing an endoplasmic reticulum (ER) leader are inserted into the ER followed by cleavage of the signal peptide. Major histocompatibility complex class I-restricted T-cell epitopes can be generated from these proteins by the proteasome after retrotranslocation into the cytosol. Here, we show that an HLA-A(*)0201-restricted epitope from prostate stem cell antigen contains the cleavage site of the ER signal peptidase. The resulting cleavage products fail to bind to HLA-A(*)0201 and are not recognized by T lymphocytes. As processing of prostate stem cell antigen by signal peptidase occurs immediately after co-translational insertion, the epitope must be processed from polypeptides that have never reached the ER. The processing of this epitope depends on the proteasome and the transporter associated with antigen processing and shows a novel pathway of class I processing that relies on the failure of ER-targeted proteins to reach their target compartment.
机译:蛋白质轴承的内质网(ER)领导人被插入到ER紧随其后信号肽的乳沟。组织相容性复合体类I-restricted从这些可以生成t细胞抗原表位蛋白质的蛋白酶体retrotranslocation进入胞液。表明0201 -限制表位抗原(*)前列腺干细胞抗原包含乳沟ER信号肽酶。乳沟产品无法绑定到抗原(*)0201而不是被T淋巴细胞。前列腺干细胞抗原的处理信号肽酶发生后立即抗原决定部位必须co-translational插入从多肽从来没有处理达到了ER。取决于蛋白酶体和运输机与抗原处理和显示小说类我处理,依赖的途径ER-targeted蛋白质未能达到他们的目标隔间。

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