Ubiquitin-protein ligase E3A (UBE3A) mediation of viral infection and human diseases.


Journal

Virus research
ISSN: 1872-7492
Titre abrégé: Virus Res
Pays: Netherlands
ID NLM: 8410979

Informations de publication

Date de publication:
02 10 2023
Historique:
received: 05 07 2023
revised: 01 08 2023
accepted: 02 08 2023
medline: 29 8 2023
pubmed: 5 8 2023
entrez: 4 8 2023
Statut: ppublish

Résumé

The Ubiquitin-protein ligase E3A, UBE3A, also known as E6-associated protein (E6-AP), is known to play an essential role in regulating the degradation of various proteins by transferring Ub from E2 Ub conjugating enzymes to the substrate proteins. Several studies indicate that UBE3A regulates the stabilities of key viral proteins in the virus-infected cells and, thereby, the infected virus-mediated diseases, even if it were reported that UBE3A participates in non-viral-related human diseases. Furthermore, mutations such as deletions and duplications in the maternally inherited gene in the brain cause human neurodevelopmental disorders such as Angelman syndrome (AS) and autism. It is also known that UBE3A functions as a transcriptional coactivator for the expression of steroid hormone receptors. These reports establish that UBE3A is distinguished by its multitudinous functions that are paramount to viral pathology and human diseases. This review is focused on molecular mechanisms for such intensive participation of UBE3A in disease formation and virus regulation.

Identifiants

pubmed: 37541588
pii: S0168-1702(23)00153-3
doi: 10.1016/j.virusres.2023.199191
pmc: PMC10430597
pii:
doi:

Substances chimiques

Ubiquitin-Protein Ligases EC 2.3.2.27
UBE3A protein, human EC 2.3.2.26

Types de publication

Journal Article Review Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

199191

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Pankaj Chaudhary (P)

Department of Microbiology, Immunology and Genetics, School of Biomedical Sciences, University of North Texas Health Science Center, Fort Worth, TX 76107, United States. Electronic address: pankaj.chaudhary@unthsc.edu.

Jessica Proulx (J)

Department of Microbiology, Immunology and Genetics, School of Biomedical Sciences, University of North Texas Health Science Center, Fort Worth, TX 76107, United States.

In-Woo Park (IW)

Department of Microbiology, Immunology and Genetics, School of Biomedical Sciences, University of North Texas Health Science Center, Fort Worth, TX 76107, United States. Electronic address: inwoo.park@unthsc.edu.

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Classifications MeSH