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Regulation of Ubiquitin Family Signaling in Disease 2.0

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

Deadline for manuscript submissions: 20 May 2024 | Viewed by 1054

Special Issue Editor


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Guest Editor
Department of Physiological Sciences, University of Barcelona, 08907 L’Hospitalet de Llobregat (Barcelona), Spain
Interests: HERC; HECT; ubiquitin; MAPK; RAF; p53; NEURL4; ubiquitylation and cell signaling
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Special Issue Information

Dear Colleagues,

We are organizing a Special Issue of the International Journal of Molecular Sciences (IJMS) (Impact Factor: 5.923 (2020 JCR), Q1 in "Biochemistry & Molecular Biology") focused on the “Regulation of Ubiquitin Family Signaling in Disease 2.0”.

Proteins are regulated by the conjugation of ubiquitin or ubiquitin-like proteins. While a synchronized cascade of three enzyme classes (E1, E2, and E3) is responsible for conjugation, deubiquitinating enzymes (DUBs) are the proteases that remove ubiquitin or ubiquitin-like molecules. This post-translational modification marks proteins by regulating their cellular functions, including their degradation, through the proteasome or the autophagy/lysosome pathway. Thus, ubiquitination/ubiquitin-like modifications have been involved in the regulation of important cellular processes such as cell proliferation, cell differentiation, DNA damage repair, cell cycle, apoptosis, signal transduction, and vesicle traffic, among others. Dysregulation of the conjugation process has been associated with multiple diseases such as neurodegeneration, cancer, viral infections, and inflammation. Understanding the molecular mechanisms involved in all these processes and their regulation is crucial to identify potential targets for the therapeutic treatment of associated diseases.

As volume 1 of the Special Issue “Regulation of Ubiquitin Family Signaling in Disease” has been successful, we will continue to explore updates of the knowledge in the field of ubiquitin family regulation and its association with diseases. As leading researchers in this field, we would like your participation.

We would like to invite you to submit an original research article or a review paper for this Special Issue.

We appreciate your consideration and sincerely hope you will accept our invitation.

Thank you very much.

Prof. Dr. Jose Luis Rosa
Guest Editor

Manuscript Submission Information

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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.

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Keywords

  • ubiquitin
  • SUMO
  • NEDD8
  • ISG15
  • FAT10
  • ubiquitin-like proteins
  • autophagy
  • proteasome

Published Papers (1 paper)

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Research

19 pages, 4677 KiB  
Article
A Survey on the Expression of the Ubiquitin Proteasome System Components HECT- and RBR-E3 Ubiquitin Ligases and E2 Ubiquitin-Conjugating and E1 Ubiquitin-Activating Enzymes during Human Brain Development
by Stefano Magnati, Eugenio Alladio and Enrico Bracco
Int. J. Mol. Sci. 2024, 25(4), 2361; https://doi.org/10.3390/ijms25042361 - 17 Feb 2024
Viewed by 831
Abstract
Human brain development involves a tightly regulated sequence of events that starts shortly after conception and continues up to adolescence. Before birth, neurogenesis occurs, implying an extensive differentiation process, sustained by changes in the gene expression profile alongside proteome remodeling, regulated by the [...] Read more.
Human brain development involves a tightly regulated sequence of events that starts shortly after conception and continues up to adolescence. Before birth, neurogenesis occurs, implying an extensive differentiation process, sustained by changes in the gene expression profile alongside proteome remodeling, regulated by the ubiquitin proteasome system (UPS) and autophagy. The latter processes rely on the selective tagging with ubiquitin of the proteins that must be disposed of. E3 ubiquitin ligases accomplish the selective recognition of the target proteins. At the late stage of neurogenesis, the brain starts to take shape, and neurons migrate to their designated locations. After birth, neuronal myelination occurs, and, in parallel, neurons form connections among each other throughout the synaptogenesis process. Due to the malfunctioning of UPS components, aberrant brain development at the very early stages leads to neurodevelopmental disorders. Through deep data mining and analysis and by taking advantage of machine learning-based models, we mapped the transcriptomic profile of the genes encoding HECT- and ring-between-ring (RBR)-E3 ubiquitin ligases as well as E2 ubiquitin-conjugating and E1 ubiquitin-activating enzymes during human brain development, from early post-conception to adulthood. The inquiry outcomes unveiled some implications for neurodevelopment-related disorders. Full article
(This article belongs to the Special Issue Regulation of Ubiquitin Family Signaling in Disease 2.0)
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