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SUMO proteins in the cardiovascular system: friend or foe?
Post-translational modifications (PTMs) are crucial for the adaptation of various signalling pathways to ensure cellular homeostasis and proper adaptation to stress. PTM is a covalent addition of a small chemical functional group such as a phosphate group (phosphorylation), methyl group (methylation...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7585181/ https://www.ncbi.nlm.nih.gov/pubmed/33099299 http://dx.doi.org/10.1186/s12929-020-00689-0 |
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author | Shetty, Prithviraj Manohar Vijaya Rangrez, Ashraf Yusuf Frey, Norbert |
author_facet | Shetty, Prithviraj Manohar Vijaya Rangrez, Ashraf Yusuf Frey, Norbert |
author_sort | Shetty, Prithviraj Manohar Vijaya |
collection | PubMed |
description | Post-translational modifications (PTMs) are crucial for the adaptation of various signalling pathways to ensure cellular homeostasis and proper adaptation to stress. PTM is a covalent addition of a small chemical functional group such as a phosphate group (phosphorylation), methyl group (methylation), or acetyl group (acetylation); lipids like hydrophobic isoprene polymers (isoprenylation); sugars such as a glycosyl group (glycosylation); or even small peptides such as ubiquitin (ubiquitination), SUMO (SUMOylation), NEDD8 (neddylation), etc. SUMO modification changes the function and/or fate of the protein especially under stress conditions, and the consequences of this conjugation can be appreciated from development to diverse disease processes. The impact of SUMOylation in disease has not been monotonous, rather SUMO is found playing a role on both sides of the coin either facilitating or impeding disease progression. Several recent studies have implicated SUMO proteins as key regulators in various cardiovascular disorders. The focus of this review is thus to summarize the current knowledge on the role of the SUMO family in the pathophysiology of cardiovascular diseases. |
format | Online Article Text |
id | pubmed-7585181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-75851812020-10-26 SUMO proteins in the cardiovascular system: friend or foe? Shetty, Prithviraj Manohar Vijaya Rangrez, Ashraf Yusuf Frey, Norbert J Biomed Sci Review Post-translational modifications (PTMs) are crucial for the adaptation of various signalling pathways to ensure cellular homeostasis and proper adaptation to stress. PTM is a covalent addition of a small chemical functional group such as a phosphate group (phosphorylation), methyl group (methylation), or acetyl group (acetylation); lipids like hydrophobic isoprene polymers (isoprenylation); sugars such as a glycosyl group (glycosylation); or even small peptides such as ubiquitin (ubiquitination), SUMO (SUMOylation), NEDD8 (neddylation), etc. SUMO modification changes the function and/or fate of the protein especially under stress conditions, and the consequences of this conjugation can be appreciated from development to diverse disease processes. The impact of SUMOylation in disease has not been monotonous, rather SUMO is found playing a role on both sides of the coin either facilitating or impeding disease progression. Several recent studies have implicated SUMO proteins as key regulators in various cardiovascular disorders. The focus of this review is thus to summarize the current knowledge on the role of the SUMO family in the pathophysiology of cardiovascular diseases. BioMed Central 2020-10-24 /pmc/articles/PMC7585181/ /pubmed/33099299 http://dx.doi.org/10.1186/s12929-020-00689-0 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Review Shetty, Prithviraj Manohar Vijaya Rangrez, Ashraf Yusuf Frey, Norbert SUMO proteins in the cardiovascular system: friend or foe? |
title | SUMO proteins in the cardiovascular system: friend or foe? |
title_full | SUMO proteins in the cardiovascular system: friend or foe? |
title_fullStr | SUMO proteins in the cardiovascular system: friend or foe? |
title_full_unstemmed | SUMO proteins in the cardiovascular system: friend or foe? |
title_short | SUMO proteins in the cardiovascular system: friend or foe? |
title_sort | sumo proteins in the cardiovascular system: friend or foe? |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7585181/ https://www.ncbi.nlm.nih.gov/pubmed/33099299 http://dx.doi.org/10.1186/s12929-020-00689-0 |
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