دورية أكاديمية
أعرض في EDS

The translocon-associated protein (TRAP) complex regulates quality control of N-linked glycosylation during ER stress.

التفاصيل البيبلوغرافية
العنوان: The translocon-associated protein (TRAP) complex regulates quality control of N-linked glycosylation during ER stress.
المؤلفون: Phoomak C; Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06510, USA., Cui W; Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06510, USA., Hayman TJ; Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06510, USA., Yu SH; Greenwood Genetic Center, Greenwood, SC 29646, USA., Zhao P; Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30601, USA., Wells L; Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30601, USA., Steet R; Greenwood Genetic Center, Greenwood, SC 29646, USA., Contessa JN; Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06510, USA. joseph.contessa@yale.edu.; Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510, USA.
المصدر: Science advances [Sci Adv] 2021 Jan 15; Vol. 7 (3). Date of Electronic Publication: 2021 Jan 15 (Print Publication: 2021).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: PubMed not MEDLINE; MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Association for the Advancement of Science, [2015]-
مستخلص: Asparagine (N)-linked glycosylation is required for endoplasmic reticulum (ER) homeostasis, but how this co- and posttranslational modification is maintained during ER stress is unknown. Here, we introduce a fluorescence-based strategy to detect aberrant N-glycosylation in individual cells and identify a regulatory role for the heterotetrameric translocon-associated protein (TRAP) complex. Unexpectedly, cells with knockout of SSR3 or SSR4 subunits restore N-glycosylation over time concurrent with a diminished ER stress transcriptional signature. Activation of ER stress or silencing of the ER chaperone BiP exacerbates or rescues the glycosylation defects, respectively, indicating that SSR3 and SSR4 enable N-glycosylation during ER stress. Protein levels of the SSR3 subunit are ER stress and UBE2J1 dependent, revealing a mechanism that coordinates upstream N-glycosylation proficiency with downstream ER-associated degradation and proteostasis. The fidelity of N-glycosylation is not static in both nontransformed and tumor cells, and the TRAP complex regulates ER glycoprotein quality control under conditions of stress.
(Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).)
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معلومات مُعتمدة: R01 GM130915 United States GM NIGMS NIH HHS; R01 GM130915 United States GM NIGMS NIH HHS; R01 GM086524 United States GM NIGMS NIH HHS; R01 CA240418 United States CA NCI NIH HHS; R01 GM127383 United States GM NIGMS NIH HHS; UL1 TR001863 United States TR NCATS NIH HHS; R01 GM086524 United States GM NIGMS NIH HHS
تواريخ الأحداث: Date Created: 20210201 Latest Revision: 20240501
رمز التحديث: 20240501
مُعرف محوري في PubMed: PMC7810369
DOI: 10.1126/sciadv.abc6364
PMID: 33523898
قاعدة البيانات: MEDLINE
الوصف
تدمد:2375-2548
DOI:10.1126/sciadv.abc6364