Ubiquitin-specific peptidase 22 functions and its involvement in disease

Deubiquitylases remove ubiquitin moieties from different substrates to regulate protein activity and cell homeostasis. Since this posttranslational modification plays a role in several different cellular functions, its deregulation has been associated with different pathologies. Aberrant expression...

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Detalles Bibliográficos
Autores principales: Melo-Cardenas, Johanna, Zhang, Yusi, Zhang, Donna D., Fang, Deyu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2016
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5190139/
https://www.ncbi.nlm.nih.gov/pubmed/27057639
http://dx.doi.org/10.18632/oncotarget.8602
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author Melo-Cardenas, Johanna
Zhang, Yusi
Zhang, Donna D.
Fang, Deyu
author_facet Melo-Cardenas, Johanna
Zhang, Yusi
Zhang, Donna D.
Fang, Deyu
author_sort Melo-Cardenas, Johanna
collection PubMed
description Deubiquitylases remove ubiquitin moieties from different substrates to regulate protein activity and cell homeostasis. Since this posttranslational modification plays a role in several different cellular functions, its deregulation has been associated with different pathologies. Aberrant expression of the Ubiquitin-Specific Peptidase 22 (USP22) has been associated with poor cancer prognosis and neurological disorders. However, little is known about USP22 role in these pathologies or in normal physiology. This review summarizes the current knowledge about USP22 function from yeast to human and provides an overview of the possible mechanisms by which USP22 is emerging as a potential oncogene.
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spelling pubmed-51901392017-01-05 Ubiquitin-specific peptidase 22 functions and its involvement in disease Melo-Cardenas, Johanna Zhang, Yusi Zhang, Donna D. Fang, Deyu Oncotarget Review Deubiquitylases remove ubiquitin moieties from different substrates to regulate protein activity and cell homeostasis. Since this posttranslational modification plays a role in several different cellular functions, its deregulation has been associated with different pathologies. Aberrant expression of the Ubiquitin-Specific Peptidase 22 (USP22) has been associated with poor cancer prognosis and neurological disorders. However, little is known about USP22 role in these pathologies or in normal physiology. This review summarizes the current knowledge about USP22 function from yeast to human and provides an overview of the possible mechanisms by which USP22 is emerging as a potential oncogene. Impact Journals LLC 2016-04-05 /pmc/articles/PMC5190139/ /pubmed/27057639 http://dx.doi.org/10.18632/oncotarget.8602 Text en Copyright: © 2016 Melo-Cardenas et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Review
Melo-Cardenas, Johanna
Zhang, Yusi
Zhang, Donna D.
Fang, Deyu
Ubiquitin-specific peptidase 22 functions and its involvement in disease
title Ubiquitin-specific peptidase 22 functions and its involvement in disease
title_full Ubiquitin-specific peptidase 22 functions and its involvement in disease
title_fullStr Ubiquitin-specific peptidase 22 functions and its involvement in disease
title_full_unstemmed Ubiquitin-specific peptidase 22 functions and its involvement in disease
title_short Ubiquitin-specific peptidase 22 functions and its involvement in disease
title_sort ubiquitin-specific peptidase 22 functions and its involvement in disease
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5190139/
https://www.ncbi.nlm.nih.gov/pubmed/27057639
http://dx.doi.org/10.18632/oncotarget.8602
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