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ERAD and Ubiquitination 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 3399

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Guest Editor
Laboratory of Physiological Chemistry, Faculty of Pharmacy, Department of Pharmacy, Takasaki University of Health and Welfare, 60 Nakaorui-machi, Takasaki-shi, Gunmma 370-0033, Japan
Interests: cross presentation; dendritic cell; the ubiquitin proteasome system; antigen presentation
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Special Issue Information

Dear Colleagues,

Last year, we launched the Special Issue “ERAD and Ubiquitination”, in which we published two research articles and four reviews. There has since been a constant influx of exciting findings in the literature, indicating this area of research has become a hot topic. Therefore, we wish to renew this Special Issue for 2021. ERAD (endoplasmic reticulum-associated degradation) has been identified as a cellular pathway of the protein quality control system in the ER, in which proteins in the ER specifically recognized as being misfolded or unassembled undergo retrograde transport out of the ER lumen and into the cytosol, where they are ubiquitinated and then degraded by proteasomes. Ubiquitination in ERAD plays a central role in the degradation of ERAD substrates by proteasomes but also functions as a recognition signal for retro-translocation and adjustment signals between ERAD-related molecular machinery. Disorders of ERAD-related ubiquitination result from activation of the UPR (unfolded protein response), and recent investigations have revealed that the UPR plays substantial roles in tumor progression, immunity, development, and aging. In this Special Issue of IJMS, we will address the role of ubiquitination in ERAD. This Special Issue will highlight the expansion in our understanding of the numerous roles of ERAD-related ubiquitination in various processes ranging from cellular homeostasis to individual homeostasis and development.

Prof. Dr. Jun Imai
Guest Editor

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Keywords

ERAD;

ubiquitination;

CUE domain;

ubiquitin chain conformation

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Published Papers (1 paper)

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Review

17 pages, 1611 KiB  
Review
Viruses Hijack ERAD to Regulate Their Replication and Propagation
by Linke Zou, Xinyan Wang, Feifan Zhao, Keke Wu, Xiaowen Li, Zhaoyao Li, Yuwan Li, Wenxian Chen, Sen Zeng, Xiaodi Liu, Mingqiu Zhao, Lin Yi, Shuangqi Fan and Jinding Chen
Int. J. Mol. Sci. 2022, 23(16), 9398; https://doi.org/10.3390/ijms23169398 - 20 Aug 2022
Cited by 5 | Viewed by 2776
Abstract
Endoplasmic reticulum-associated degradation (ERAD) is highly conserved in yeast. Recent studies have shown that ERAD is also ubiquitous and highly conserved in eukaryotic cells, where it plays an essential role in maintaining endoplasmic reticulum (ER) homeostasis. Misfolded or unfolded proteins undergo ERAD. They [...] Read more.
Endoplasmic reticulum-associated degradation (ERAD) is highly conserved in yeast. Recent studies have shown that ERAD is also ubiquitous and highly conserved in eukaryotic cells, where it plays an essential role in maintaining endoplasmic reticulum (ER) homeostasis. Misfolded or unfolded proteins undergo ERAD. They are recognized in the ER, retrotranslocated into the cytoplasm, and degraded by proteasomes after polyubiquitin. This may consist of several main steps: recognition of ERAD substrates, retrotranslocation, and proteasome degradation. Replication and transmission of the virus in the host is a process of a “game” with the host. It can be assumed that the virus has evolved various mechanisms to use the host’s functions for its replication and transmission, including ERAD. However, until now, it is still unclear how the host uses ERAD to deal with virus infection and how the viruses hijack the function of ERAD to obtain a favorable niche or evade the immune clearance of the host. Recent studies have shown that viruses have also evolved mechanisms to use various processes of ERAD to promote their transmission. This review describes the occurrence of ERAD and how the viruses hijack the function of ERAD to spread by affecting the homeostasis and immune response of the host, and we will focus on the role of E3 ubiquitin ligase. Full article
(This article belongs to the Special Issue ERAD and Ubiquitination 2.0)
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