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Post-translational modifications of PML: consequences and implications
The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regu...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539660/ https://www.ncbi.nlm.nih.gov/pubmed/23316480 http://dx.doi.org/10.3389/fonc.2012.00210 |
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author | Cheng, Xiwen Kao, Hung-Ying |
author_facet | Cheng, Xiwen Kao, Hung-Ying |
author_sort | Cheng, Xiwen |
collection | PubMed |
description | The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regulation in response to stress and environmental cues are not complete. Post-translational modifications, such as SUMOylation, phosphorylation, acetylation, and ubiquitination of PML add a complex layer of regulation to the physiological function of PML. In this review, we discuss the fast-moving horizon of post-translational modifications targeting PML. |
format | Online Article Text |
id | pubmed-3539660 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-35396602013-01-11 Post-translational modifications of PML: consequences and implications Cheng, Xiwen Kao, Hung-Ying Front Oncol Oncology The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regulation in response to stress and environmental cues are not complete. Post-translational modifications, such as SUMOylation, phosphorylation, acetylation, and ubiquitination of PML add a complex layer of regulation to the physiological function of PML. In this review, we discuss the fast-moving horizon of post-translational modifications targeting PML. Frontiers Media S.A. 2013-01-04 /pmc/articles/PMC3539660/ /pubmed/23316480 http://dx.doi.org/10.3389/fonc.2012.00210 Text en Copyright © Cheng and Kao. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc. |
spellingShingle | Oncology Cheng, Xiwen Kao, Hung-Ying Post-translational modifications of PML: consequences and implications |
title | Post-translational modifications of PML: consequences and implications |
title_full | Post-translational modifications of PML: consequences and implications |
title_fullStr | Post-translational modifications of PML: consequences and implications |
title_full_unstemmed | Post-translational modifications of PML: consequences and implications |
title_short | Post-translational modifications of PML: consequences and implications |
title_sort | post-translational modifications of pml: consequences and implications |
topic | Oncology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539660/ https://www.ncbi.nlm.nih.gov/pubmed/23316480 http://dx.doi.org/10.3389/fonc.2012.00210 |
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