Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.

p44/MEP50/WDR77 has been identified as a coactivator of androgen receptor (AR), with distinct growth suppression and promotion function in gender specific endocrine organs and their malignancies. We dissected the functional domains of p44 for protein interaction with transcription factors, transcrip...

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Autores principales: Yirong Li, Liantian Tian, Martin Ligr, Garrett Daniels, Yi Peng, Xinyu Wu, Mandeep Singh, Jianjun Wei, Yongzhao Shao, Herbert Lepor, Ruliang Xu, Zhijie Chang, Zhengxin Wang, Peng Lee
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Publicado: Public Library of Science (PLoS) 2013
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Acceso en línea:https://doaj.org/article/a171e214df7948f19f0b7260eaa0733f
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spelling oai:doaj.org-article:a171e214df7948f19f0b7260eaa0733f2021-11-18T07:43:55ZFunctional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.1932-620310.1371/journal.pone.0064663https://doaj.org/article/a171e214df7948f19f0b7260eaa0733f2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23734213/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203p44/MEP50/WDR77 has been identified as a coactivator of androgen receptor (AR), with distinct growth suppression and promotion function in gender specific endocrine organs and their malignancies. We dissected the functional domains of p44 for protein interaction with transcription factors, transcriptional activation, as well as the functional domains in p44 related to its growth inhibition in prostate cancer. Using a yeast two-hybrid screen, we identified a novel transcription complex AR-p44-Smad1, confirmed for physical interaction by co-immunoprecipitaion and functional interaction with luciferase assays in human prostate cancer cells. Yeast two-hybrid assay revealed that the N-terminal region of p44, instead of the traditional WD40 domain at the C-terminus, mediates the interaction among p44, N-terminus of AR and full length Smad1. Although both N and C terminal domains of p44 are necessary for maximum AR transcriptional activation, the N terminal fragment of p44 alone maintains the basic effect on AR transcriptional activation. Cell proliferation assays with N- and C- terminal deletion mutations indicated that the central portion of p44 is required for nuclear p44 mediated prostate cancer growth inhibition.Yirong LiLiantian TianMartin LigrGarrett DanielsYi PengXinyu WuMandeep SinghJianjun WeiYongzhao ShaoHerbert LeporRuliang XuZhijie ChangZhengxin WangPeng LeePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e64663 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Yirong Li
Liantian Tian
Martin Ligr
Garrett Daniels
Yi Peng
Xinyu Wu
Mandeep Singh
Jianjun Wei
Yongzhao Shao
Herbert Lepor
Ruliang Xu
Zhijie Chang
Zhengxin Wang
Peng Lee
Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
description p44/MEP50/WDR77 has been identified as a coactivator of androgen receptor (AR), with distinct growth suppression and promotion function in gender specific endocrine organs and their malignancies. We dissected the functional domains of p44 for protein interaction with transcription factors, transcriptional activation, as well as the functional domains in p44 related to its growth inhibition in prostate cancer. Using a yeast two-hybrid screen, we identified a novel transcription complex AR-p44-Smad1, confirmed for physical interaction by co-immunoprecipitaion and functional interaction with luciferase assays in human prostate cancer cells. Yeast two-hybrid assay revealed that the N-terminal region of p44, instead of the traditional WD40 domain at the C-terminus, mediates the interaction among p44, N-terminus of AR and full length Smad1. Although both N and C terminal domains of p44 are necessary for maximum AR transcriptional activation, the N terminal fragment of p44 alone maintains the basic effect on AR transcriptional activation. Cell proliferation assays with N- and C- terminal deletion mutations indicated that the central portion of p44 is required for nuclear p44 mediated prostate cancer growth inhibition.
format article
author Yirong Li
Liantian Tian
Martin Ligr
Garrett Daniels
Yi Peng
Xinyu Wu
Mandeep Singh
Jianjun Wei
Yongzhao Shao
Herbert Lepor
Ruliang Xu
Zhijie Chang
Zhengxin Wang
Peng Lee
author_facet Yirong Li
Liantian Tian
Martin Ligr
Garrett Daniels
Yi Peng
Xinyu Wu
Mandeep Singh
Jianjun Wei
Yongzhao Shao
Herbert Lepor
Ruliang Xu
Zhijie Chang
Zhengxin Wang
Peng Lee
author_sort Yirong Li
title Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
title_short Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
title_full Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
title_fullStr Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
title_full_unstemmed Functional domains of androgen receptor coactivator p44/Mep50/WDR77and its interaction with Smad1.
title_sort functional domains of androgen receptor coactivator p44/mep50/wdr77and its interaction with smad1.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/a171e214df7948f19f0b7260eaa0733f
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