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Developing Practical Therapeutic Strategies that Target Protein SUMOylation

Post-translational modification by small ubiquitin-like modifier (SUMO) has emerged as a global mechanism for the control and integration of a wide variety of biological processes through the regulation of protein activity, stability and intracellular localization. As SUMOylation is examined in grea...

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Autores principales: Cox, Olivia F., Huber, Paul W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Science Publishers 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6700758/
https://www.ncbi.nlm.nih.gov/pubmed/30362419
http://dx.doi.org/10.2174/1389450119666181026151802
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author Cox, Olivia F.
Huber, Paul W.
author_facet Cox, Olivia F.
Huber, Paul W.
author_sort Cox, Olivia F.
collection PubMed
description Post-translational modification by small ubiquitin-like modifier (SUMO) has emerged as a global mechanism for the control and integration of a wide variety of biological processes through the regulation of protein activity, stability and intracellular localization. As SUMOylation is examined in greater detail, it has become clear that the process is at the root of several pathologies including heart, endocrine, and inflammatory disease, and various types of cancer. Moreover, it is certain that perturba-tion of this process, either globally or of a specific protein, accounts for many instances of congenital birth defects. In order to be successful, practical strategies to ameliorate conditions due to disruptions in this post-translational modification will need to consider the multiple components of the SUMOylation machinery and the extraordinary number of proteins that undergo this modification.
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spelling pubmed-67007582019-11-18 Developing Practical Therapeutic Strategies that Target Protein SUMOylation Cox, Olivia F. Huber, Paul W. Curr Drug Targets Article Post-translational modification by small ubiquitin-like modifier (SUMO) has emerged as a global mechanism for the control and integration of a wide variety of biological processes through the regulation of protein activity, stability and intracellular localization. As SUMOylation is examined in greater detail, it has become clear that the process is at the root of several pathologies including heart, endocrine, and inflammatory disease, and various types of cancer. Moreover, it is certain that perturba-tion of this process, either globally or of a specific protein, accounts for many instances of congenital birth defects. In order to be successful, practical strategies to ameliorate conditions due to disruptions in this post-translational modification will need to consider the multiple components of the SUMOylation machinery and the extraordinary number of proteins that undergo this modification. Bentham Science Publishers 2019-07 2019-07 /pmc/articles/PMC6700758/ /pubmed/30362419 http://dx.doi.org/10.2174/1389450119666181026151802 Text en © 2019 Bentham Science Publishers https://creativecommons.org/licenses/by-nc/4.0/legalcode This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Cox, Olivia F.
Huber, Paul W.
Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title_full Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title_fullStr Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title_full_unstemmed Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title_short Developing Practical Therapeutic Strategies that Target Protein SUMOylation
title_sort developing practical therapeutic strategies that target protein sumoylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6700758/
https://www.ncbi.nlm.nih.gov/pubmed/30362419
http://dx.doi.org/10.2174/1389450119666181026151802
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