دورية أكاديمية

The unfolded protein response and endoplasmic reticulum protein targeting machineries converge on the stress sensor IRE1

التفاصيل البيبلوغرافية
العنوان: The unfolded protein response and endoplasmic reticulum protein targeting machineries converge on the stress sensor IRE1
المؤلفون: Diego Acosta-Alvear, G Elif Karagöz, Florian Fröhlich, Han Li, Tobias C Walther, Peter Walter
المصدر: eLife, Vol 7 (2018)
بيانات النشر: eLife Sciences Publications Ltd, 2018.
سنة النشر: 2018
المجموعة: LCC:Medicine
LCC:Science
LCC:Biology (General)
مصطلحات موضوعية: unfolded protein response, co-translational protein targeting, IRE1, RNA-protein interactome, ribosome, endoplasmic reticulum, Medicine, Science, Biology (General), QH301-705.5
الوصف: The protein folding capacity of the endoplasmic reticulum (ER) is tightly regulated by a network of signaling pathways, known as the unfolded protein response (UPR). UPR sensors monitor the ER folding status to adjust ER folding capacity according to need. To understand how the UPR sensor IRE1 maintains ER homeostasis, we identified zero-length crosslinks of RNA to IRE1 with single nucleotide precision in vivo. We found that IRE1 specifically crosslinks to a subset of ER-targeted mRNAs, SRP RNA, ribosomal and transfer RNAs. Crosslink sites cluster in a discrete region of the ribosome surface spanning from the A-site to the polypeptide exit tunnel. Moreover, IRE1 binds to purified 80S ribosomes with high affinity, indicating association with ER-bound ribosomes. Our results suggest that the ER protein translocation and targeting machineries work together with the UPR to tune the ER’s protein folding load.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2050-084X
Relation: https://elifesciences.org/articles/43036; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.43036
URL الوصول: https://doaj.org/article/2d8761a557fe4bf0ac216cfdf1d5ec8b
رقم الأكسشن: edsdoj.2d8761a557fe4bf0ac216cfdf1d5ec8b
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2050084X
DOI:10.7554/eLife.43036