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UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10

Questions have been raised since the discovery of UBA6 and its significant coexistence with UBE1 in the ubiquitin–proteasome system (UPS). The facts that UBA6 has the dedicated E2 enzyme USE1 and the E1–E2 cascade can activate and transfer both ubiquitin and ubiquitin-like protein FAT10 have attract...

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Detalles Bibliográficos
Autores principales: Wang, Fengting, Zhao, Bo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539292/
https://www.ncbi.nlm.nih.gov/pubmed/31067743
http://dx.doi.org/10.3390/ijms20092250
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author Wang, Fengting
Zhao, Bo
author_facet Wang, Fengting
Zhao, Bo
author_sort Wang, Fengting
collection PubMed
description Questions have been raised since the discovery of UBA6 and its significant coexistence with UBE1 in the ubiquitin–proteasome system (UPS). The facts that UBA6 has the dedicated E2 enzyme USE1 and the E1–E2 cascade can activate and transfer both ubiquitin and ubiquitin-like protein FAT10 have attracted a great deal of attention to the regulational mechanisms of the UBA6–USE1 cascade and to how FAT10 and ubiquitin differentiate with each other. This review recapitulates the latest advances in UBA6 and its bispecific UBA6–USE1 pathways for both ubiquitin and FAT10. The intricate networks of UBA6 and its interplays with ubiquitin and FAT10 are briefly reviewed, as are their individual and collective functions in diverse physiological conditions.
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spelling pubmed-65392922019-06-04 UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10 Wang, Fengting Zhao, Bo Int J Mol Sci Review Questions have been raised since the discovery of UBA6 and its significant coexistence with UBE1 in the ubiquitin–proteasome system (UPS). The facts that UBA6 has the dedicated E2 enzyme USE1 and the E1–E2 cascade can activate and transfer both ubiquitin and ubiquitin-like protein FAT10 have attracted a great deal of attention to the regulational mechanisms of the UBA6–USE1 cascade and to how FAT10 and ubiquitin differentiate with each other. This review recapitulates the latest advances in UBA6 and its bispecific UBA6–USE1 pathways for both ubiquitin and FAT10. The intricate networks of UBA6 and its interplays with ubiquitin and FAT10 are briefly reviewed, as are their individual and collective functions in diverse physiological conditions. MDPI 2019-05-07 /pmc/articles/PMC6539292/ /pubmed/31067743 http://dx.doi.org/10.3390/ijms20092250 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Wang, Fengting
Zhao, Bo
UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title_full UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title_fullStr UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title_full_unstemmed UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title_short UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10
title_sort uba6 and its bispecific pathways for ubiquitin and fat10
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539292/
https://www.ncbi.nlm.nih.gov/pubmed/31067743
http://dx.doi.org/10.3390/ijms20092250
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