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The Ubiquitination Machinery: Its Versatile Role in Normal and Disease-Related Cellular Processes

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

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 13904

Special Issue Editors

Dr. Peter Deak

E-Mail Website
Guest Editor
Department of Genetics, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary
Interests: ubiquitin-proteasome system; role of the Anaphase Promoting Complex/Ciclosome (APC/C) in cell cycle regulation; functional analysis of deubiquitylating enzymes; Drosophila molecular genetics; disease models in Drosophila
Dr. Yuu Yuu Kimata

E-Mail
Guest Editor
School of Life Science and Technology, ShanghaiTech University, Shanghai, China
Dr. Levente Kovács

E-Mail
Guest Editor
Division of Biology and Biological Engineering, California Institute of Technolgy, Pasadena, CA 91125, USA

Special Issue Information

Dear Colleagues,

Ubiquitination is a widespread and reversible post-translational modification of eukaryotic proteins, in which ubiquitin (Ub) or ubiquitin-like proteins (UbL) are conjugated to protein substrates by an enzyme cascade. The Ub and UbL marks are only transient, since deubiquitinating enzymes (DUBs) hydrolyze the covalent bonds linking these marks to substrates. The Ub and UbL functional interplay modulates protein stability, activity or localization, or protein–protein interaction, thus representing a dynamic system that vitally regulates an increasing number of cellular processes. Simultaneous ubiquitin-dependent processes compete for limited Ub and UbL pools and, thus, must be tightly coordinated by constant ubiquitination-deubiquitination cycles.

Several decades of research pinned down many components, substrates, and regulatory pathways of the highly complex ubiquitination machinery. Various disruptions of this system are implicated in the genesis of many human diseases, such as neurodegeneration, inflammation, or cancer. Therefore, a better understanding of the ubiquitination system is crucial for developing therapeutic or preventative measures against these diseases.

In this Special Issue of the International Journal of Molecular Sciences, we would like to invite contributions addressing the functional analysis of ubiquitination machinery components or identifying new substrates or regulatory circuits, with an emphasis on pathological implications or therapeutic prospects. Submissions can either be original research papers or reviews. Your contributions will be highly appreciated.

Dr. Peter Deak
Dr. Yuu Kimata
Dr. Levente Kovács
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ubiquitin and ubiquitin-like proteins (such as SUMO, NEDD8, ISG15, Apg12, FAT10, etc.)
  • ubiquitylation and deubiquitylation
  • selective proteolysis and protein homeostasis
  • E1 ubiquitin-activating enzyme
  • E2 ubiquitin-conjugating enzyme
  • E3 ubiquitin ligases
  • deubiquitylases
  • ubiquitin cycle
  • cell cycle regulation
  • disease association
  • disease model
  • stem cells

Published Papers (3 papers)

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Research

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13 pages, 2458 KiB  
Article
Deubiquitinating Enzyme USP8 Is Essential for Skeletogenesis by Regulating Wnt Signaling
by Sachin Chaugule, Jung-Min Kim, Yeon-Suk Yang, Klaus-Peter Knobeloch, Xi He and Jae-Hyuck Shim
Int. J. Mol. Sci. 2021, 22(19), 10289; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms221910289 - 24 Sep 2021
Cited by 3 | Viewed by 2227
Abstract
Disturbance in a differentiation program of skeletal stem cells leads to indecorous skeletogenesis. Growing evidence suggests that a fine-tuning of ubiquitin-mediated protein degradation is crucial for skeletal stem cells to maintain their stemness and osteogenic potential. Here, we demonstrate that the deubiquitinating enzyme [...] Read more.
Disturbance in a differentiation program of skeletal stem cells leads to indecorous skeletogenesis. Growing evidence suggests that a fine-tuning of ubiquitin-mediated protein degradation is crucial for skeletal stem cells to maintain their stemness and osteogenic potential. Here, we demonstrate that the deubiquitinating enzyme (DUB) ubiquitin-specific protease 8 (USP8) stabilizes the Wnt receptor frizzled 5 (FZD5) by preventing its lysosomal degradation. This pathway is essential for Wnt/β-catenin signaling and the differentiation of osteoprogenitors to mature osteoblasts. Accordingly, deletion of USP8 in osteoprogenitors (Usp8Osx) resulted in a near-complete blockade in skeletal mineralization, similar to that seen in mice with defective Wnt/β-catenin signaling. Likewise, transplanting USP8-deficient osteoprogenitors under the renal capsule in wild-type secondary hosts did not to induce bone formation. Collectively, this study unveils an essential role for the DUB USP8 in Wnt/β-catenin signaling in osteoprogenitors and osteogenesis during skeletal development. Full article
(This article belongs to the Special Issue The Ubiquitination Machinery: Its Versatile Role in Normal and Disease-Related Cellular Processes)
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Review

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13 pages, 1632 KiB  
Review
UBL5/Hub1: An Atypical Ubiquitin-Like Protein with a Typical Role as a Stress-Responsive Regulator
by Sittinan Chanarat
Int. J. Mol. Sci. 2021, 22(17), 9384; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22179384 - 30 Aug 2021
Cited by 7 | Viewed by 3231
Abstract
Members of the ubiquitin-like protein family are known for their ability to modify substrates by covalent conjugation. The highly conserved ubiquitin relative UBL5/Hub1, however, is atypical because it lacks a carboxy-terminal di-glycine motif required for conjugation, and the whole E1-E2-E3 enzyme cascade is [...] Read more.
Members of the ubiquitin-like protein family are known for their ability to modify substrates by covalent conjugation. The highly conserved ubiquitin relative UBL5/Hub1, however, is atypical because it lacks a carboxy-terminal di-glycine motif required for conjugation, and the whole E1-E2-E3 enzyme cascade is likely absent. Though the conjugation-mediated role of UBL5/Hub1 is controversial, it undoubtedly functions by interacting non-covalently with its partners. Several interactors of UBL5/Hub1 identified to date have suggested broad stress-responsive functions of the protein, for example, stress-induced control of pre-mRNA splicing, Fanconi anemia pathway of DNA damage repair, and mitochondrial unfolded protein response. While having an atypical mode of function, UBL5/Hub1 is still a stress protein that regulates feedback to various stimuli in a similar manner to other ubiquitin-like proteins. In this review, I discuss recent progress in understanding the functions of UBL5/Hub1 and the fundamental questions which remain to be answered. Full article
(This article belongs to the Special Issue The Ubiquitination Machinery: Its Versatile Role in Normal and Disease-Related Cellular Processes)
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26 pages, 1164 KiB  
Review
The Involvement of Ubiquitination Machinery in Cell Cycle Regulation and Cancer Progression
by Tingting Zou and Zhenghong Lin
Int. J. Mol. Sci. 2021, 22(11), 5754; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22115754 - 27 May 2021
Cited by 41 | Viewed by 7199
Abstract
The cell cycle is a collection of events by which cellular components such as genetic materials and cytoplasmic components are accurately divided into two daughter cells. The cell cycle transition is primarily driven by the activation of cyclin-dependent kinases (CDKs), which activities are [...] Read more.
The cell cycle is a collection of events by which cellular components such as genetic materials and cytoplasmic components are accurately divided into two daughter cells. The cell cycle transition is primarily driven by the activation of cyclin-dependent kinases (CDKs), which activities are regulated by the ubiquitin-mediated proteolysis of key regulators such as cyclins, CDK inhibitors (CKIs), other kinases and phosphatases. Thus, the ubiquitin-proteasome system (UPS) plays a pivotal role in the regulation of the cell cycle progression via recognition, interaction, and ubiquitination or deubiquitination of key proteins. The illegitimate degradation of tumor suppressor or abnormally high accumulation of oncoproteins often results in deregulation of cell proliferation, genomic instability, and cancer occurrence. In this review, we demonstrate the diversity and complexity of the regulation of UPS machinery of the cell cycle. A profound understanding of the ubiquitination machinery will provide new insights into the regulation of the cell cycle transition, cancer treatment, and the development of anti-cancer drugs. Full article
(This article belongs to the Special Issue The Ubiquitination Machinery: Its Versatile Role in Normal and Disease-Related Cellular Processes)
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