Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.

Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.
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信号识别颗粒受体-β (SR-β) 协调共翻译 N-糖基化。

DOI:
10.1126/sciadv.ade8079
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发表时间:
2023-03-17
期刊:
影响因子:
13.6
通讯作者:
Contessa, Joseph N.
Contessa, Joseph N.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Phoomak, Chatchai;Rinis, Natalie;Baro, Marta;Shrimal, Shiteshu;Bennett, Daniel;Shaffer, Scott A.;Lehrman, Mark;Gilmore, Reid;Contessa, Joseph N.

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预定用于细胞分泌区的蛋白质被协同转运到内质网中。这些蛋白质中的大多数是N-糖基化的,这是一种共翻译和翻译后修饰,可确保蛋白质正确折叠、稳定性、溶解性和细胞定位。在这里,我们表明,信号识别颗粒受体(SR)的亚基是必需的N-糖基化能力的易位子的组装。我们报告说,鸟嘌呤类似物化学探针鉴定的高通量筛选或突变的SR-鸟苷三磷酸结合位点引起的N-糖基化缺陷的表型。这两种方法都没有改变SR-与SR-的关联,但这两种方法都减少了SR-与寡糖基转移酶复合物的关联。这些实验证明SR-具有先前未被认识到的协调内质网翻译与N-糖基化的功能。RNC复合物向有N-糖基化能力的易位子的移交依赖于OST的SR促进的募集。
Proteins destined for the secretory compartment of the cell are cotranslationally translocated into the endoplasmic reticulum. The majority of these proteins are N-glycosylated, a co- and posttranslational modification that ensures proper protein folding, stability, solubility, and cellular localization. Here, we show that the subunit of the signal recognition particle receptor (SR) is required for assembly of the N-glycosylation–competent translocon. We report that guanine analog chemical probes identified by high-throughput screening or mutation of the SR- guanosine triphosphate binding site cause an N-glycosylation–deficient phenotype. Neither method alters the association of SR- with SR-, but both approaches reduce the association of SR- with the oligosaccharyltransferase complex. These experiments demonstrate that SR- has a previously unrecognized function coordinating endoplasmic reticulum translation with N-glycosylation. Handover of the RNC complex to an N-glycosylation competent translocon is dependent on SR- facilitated recruitment of the OST.
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