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Proline-Directed Androgen Receptor Phosphorylation
The androgen receptor (AR) has been identified for decades and mediates essential steroid functions. Like most of biological molecules, AR functional activities are modulated by post-translational modifications. This review is focused on the reported activities and significance of AR phosphorylation...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4389684/ https://www.ncbi.nlm.nih.gov/pubmed/25866551 http://dx.doi.org/10.4172/1747-0862.1000075 |
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author | Gao, Yanfei Chen, Shaoyong |
author_facet | Gao, Yanfei Chen, Shaoyong |
author_sort | Gao, Yanfei |
collection | PubMed |
description | The androgen receptor (AR) has been identified for decades and mediates essential steroid functions. Like most of biological molecules, AR functional activities are modulated by post-translational modifications. This review is focused on the reported activities and significance of AR phosphorylation, with particular emphasis on proline-directed serine/threonine phosphorylation that occurs predominantly on the receptor. The marked enrichment of AR phosphorylation in the most diverse N-terminal domain suggests that targeting AR phosphorylation can be synergistic to antagonizing the C-terminal domain by clinical antiandrogens. |
format | Online Article Text |
id | pubmed-4389684 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-43896842015-04-08 Proline-Directed Androgen Receptor Phosphorylation Gao, Yanfei Chen, Shaoyong J Mol Genet Med Article The androgen receptor (AR) has been identified for decades and mediates essential steroid functions. Like most of biological molecules, AR functional activities are modulated by post-translational modifications. This review is focused on the reported activities and significance of AR phosphorylation, with particular emphasis on proline-directed serine/threonine phosphorylation that occurs predominantly on the receptor. The marked enrichment of AR phosphorylation in the most diverse N-terminal domain suggests that targeting AR phosphorylation can be synergistic to antagonizing the C-terminal domain by clinical antiandrogens. 2013-08-26 2013-10 /pmc/articles/PMC4389684/ /pubmed/25866551 http://dx.doi.org/10.4172/1747-0862.1000075 Text en © 2013 Gao Y, et al. http://creativecommons.org/licenses/by/2.0/ 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 | Article Gao, Yanfei Chen, Shaoyong Proline-Directed Androgen Receptor Phosphorylation |
title | Proline-Directed Androgen Receptor Phosphorylation |
title_full | Proline-Directed Androgen Receptor Phosphorylation |
title_fullStr | Proline-Directed Androgen Receptor Phosphorylation |
title_full_unstemmed | Proline-Directed Androgen Receptor Phosphorylation |
title_short | Proline-Directed Androgen Receptor Phosphorylation |
title_sort | proline-directed androgen receptor phosphorylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4389684/ https://www.ncbi.nlm.nih.gov/pubmed/25866551 http://dx.doi.org/10.4172/1747-0862.1000075 |
work_keys_str_mv | AT gaoyanfei prolinedirectedandrogenreceptorphosphorylation AT chenshaoyong prolinedirectedandrogenreceptorphosphorylation |