Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.

Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.
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DOI:
10.3390/ijms23010281
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发表时间:
2021-12-28
影响因子:
5.6
通讯作者:
Shan SO
Shan SO
中科院分区:
生物学2区
文献类型:
--
作者:
Hsieh HH;Shan SO

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蛋白质靶向的保真度对细胞器的正常生物发生和功能至关重要。与复制、转录和翻译过程不同,在这些过程中,识别和拒绝非同源底物的多种机制是在能量和分子细节上建立起来的,细胞在蛋白质定位中实现高保真度的机制仍然不完全清楚。信号识别粒子(Signal recognition particle, SRP)是一种介导细胞膜和分泌蛋白定位到合适细胞膜的保守途径,为理解细胞中蛋白质定位的分子基础提供了一种范式。在本章中,我们回顾了最近在哺乳动物SRP途径的分子机制和底物选择方面的研究进展,重点介绍了协译伴侣NAC在防止蛋白质错靶向内质网和确保蛋白质定位的细胞器特异性方面的关键作用。
Fidelity of protein targeting is essential for the proper biogenesis and functioning of organelles. Unlike replication, transcription and translation processes, in which multiple mechanisms to recognize and reject noncognate substrates are established in energetic and molecular detail, the mechanisms by which cells achieve a high fidelity in protein localization remain incompletely understood. Signal recognition particle (SRP), a conserved pathway to mediate the localization of membrane and secretory proteins to the appropriate cellular membrane, provides a paradigm to understand the molecular basis of protein localization in the cell. In this chapter, we review recent progress in deciphering the molecular mechanisms and substrate selection of the mammalian SRP pathway, with an emphasis on the key role of the cotranslational chaperone NAC in preventing protein mistargeting to the ER and in ensuring the organelle specificity of protein localization.
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