دورية أكاديمية

Turnover of EDEM1, an ERAD-enhancing factor, is mediated by multiple degradation routes.

التفاصيل البيبلوغرافية
العنوان: Turnover of EDEM1, an ERAD-enhancing factor, is mediated by multiple degradation routes.
المؤلفون: Katsuki R; Department of Life Science, Graduated School of Engineering Science, Akita University, Akita, Japan., Kanuka M; Department of Life Science, Graduated School of Engineering Science, Akita University, Akita, Japan., Ohta R; Department of Life Science, Graduated School of Engineering Science, Akita University, Akita, Japan., Yoshida S; Department of Life Science, Faculty of Engineering Science, Akita University, Akita, Japan., Tamura T; Department of Life Science, Graduated School of Engineering Science, Akita University, Akita, Japan.; Department of Life Science, Faculty of Engineering Science, Akita University, Akita, Japan.
المصدر: Genes to cells : devoted to molecular & cellular mechanisms [Genes Cells] 2024 Jun; Vol. 29 (6), pp. 486-502. Date of Electronic Publication: 2024 Apr 29.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Blackwell Science Ltd Country of Publication: England NLM ID: 9607379 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1365-2443 (Electronic) Linking ISSN: 13569597 NLM ISO Abbreviation: Genes Cells Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Oxford, UK : Blackwell Science Ltd., 1996-
مواضيع طبية MeSH: Endoplasmic Reticulum-Associated Degradation* , Membrane Proteins*/metabolism , Membrane Proteins*/genetics , Autophagy* , Endoplasmic Reticulum*/metabolism, Humans ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Protein Folding ; HEK293 Cells ; Endoplasmic Reticulum Stress ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitin-Protein Ligases/genetics ; Proteins
مستخلص: Quality-based protein production and degradation in the endoplasmic reticulum (ER) are essential for eukaryotic cell survival. During protein maturation in the ER, misfolded or unassembled proteins are destined for disposal through a process known as ER-associated degradation (ERAD). EDEM1 is an ERAD-accelerating factor whose gene expression is upregulated by the accumulation of aberrant proteins in the ER, known as ER stress. Although the role of EDEM1 in ERAD has been studied in detail, the turnover of EDEM1 by intracellular degradation machinery, including the proteasome and autophagy, is not well understood. To clarify EDEM1 regulation in the protein level, degradation mechanism of EDEM1 was examined. Our results indicate that both ERAD and autophagy degrade EDEM1 alike misfolded degradation substrates, although each degradation machinery targets EDEM1 in different folded states of proteins. We also found that ERAD factors, including the SEL1L/Hrd1 complex, YOD1, XTP3B, ERdj3, VIMP, BAG6, and JB12, but not OS9, are involved in EDEM1 degradation in a mannose-trimming-dependent and -independent manner. Our results suggest that the ERAD accelerating factor, EDEM1, is turned over by the ERAD itself, similar to ERAD clients.
(© 2024 The Authors. Genes to Cells published by Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.)
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فهرسة مساهمة: Keywords: EDEM1; ER quality control; ER stress; ERAD; autophagy; proteasome; protein degradation; protein turnover; unfolded protein response
المشرفين على المادة: 0 (EDEM1 protein, human)
0 (Membrane Proteins)
EC 3.4.25.1 (Proteasome Endopeptidase Complex)
0 (SEL1L protein, human)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
0 (Proteins)
تواريخ الأحداث: Date Created: 20240429 Date Completed: 20240610 Latest Revision: 20240617
رمز التحديث: 20240617
مُعرف محوري في PubMed: PMC11163939
DOI: 10.1111/gtc.13117
PMID: 38682256
قاعدة البيانات: MEDLINE