Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Cheng, Xiwen, Kao, Hung-Ying
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
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
_version_ 1782255131011579904
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
work_keys_str_mv AT chengxiwen posttranslationalmodificationsofpmlconsequencesandimplications
AT kaohungying posttranslationalmodificationsofpmlconsequencesandimplications