Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription

Abstract Steroid receptor coactivator-3 (SRC-3) regulates the activity of both nuclear hormone receptors and a number of key transcription factors. It is implicated in the regulation of cell proliferation, inflammation and in the progression of several common cancers including breast, colorectal and...

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Autores principales:	Anup Shrestha, Henrike Bruckmueller, Hanne Kildalsen, Gurjit Kaur, Matthias Gaestel, Hilde Ljones Wetting, Ingvild Mikkola, Ole-Morten Seternes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0e455ff65b5a4346bcb8398d6c90b6fa
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spelling	oai:doaj.org-article:0e455ff65b5a4346bcb8398d6c90b6fa2021-12-02T15:39:49ZPhosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription10.1038/s41598-020-68219-42045-2322https://doaj.org/article/0e455ff65b5a4346bcb8398d6c90b6fa2020-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-68219-4https://doaj.org/toc/2045-2322Abstract Steroid receptor coactivator-3 (SRC-3) regulates the activity of both nuclear hormone receptors and a number of key transcription factors. It is implicated in the regulation of cell proliferation, inflammation and in the progression of several common cancers including breast, colorectal and lung tumors. Phosphorylation is an important regulatory event controlling the activities of SRC-3. Serine 857 is the most studied phospho-acceptor site, and its modification has been reported to be important for SRC-3-dependent tumor progression. In this study, we show that the stress-responsive p38MAPK-MK2 signaling pathway controls the phosphorylation of SRC-3 at S857 in a wide range of human cancer cells. Activation of the p38MAPK-MK2 pathway results in the nuclear translocation of SRC-3, where it contributes to the transactivation of NF-kB and thus regulation of IL-6 transcription. The identification of the p38MAPK-MK2 signaling axis as a key regulator of SRC-3 phosphorylation and activity opens up new possibilities for the development and testing of novel therapeutic strategies to control both proliferative and metastatic tumor growth.Anup ShresthaHenrike BruckmuellerHanne KildalsenGurjit KaurMatthias GaestelHilde Ljones WettingIngvild MikkolaOle-Morten SeternesNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-22 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anup Shrestha Henrike Bruckmueller Hanne Kildalsen Gurjit Kaur Matthias Gaestel Hilde Ljones Wetting Ingvild Mikkola Ole-Morten Seternes Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
description	Abstract Steroid receptor coactivator-3 (SRC-3) regulates the activity of both nuclear hormone receptors and a number of key transcription factors. It is implicated in the regulation of cell proliferation, inflammation and in the progression of several common cancers including breast, colorectal and lung tumors. Phosphorylation is an important regulatory event controlling the activities of SRC-3. Serine 857 is the most studied phospho-acceptor site, and its modification has been reported to be important for SRC-3-dependent tumor progression. In this study, we show that the stress-responsive p38MAPK-MK2 signaling pathway controls the phosphorylation of SRC-3 at S857 in a wide range of human cancer cells. Activation of the p38MAPK-MK2 pathway results in the nuclear translocation of SRC-3, where it contributes to the transactivation of NF-kB and thus regulation of IL-6 transcription. The identification of the p38MAPK-MK2 signaling axis as a key regulator of SRC-3 phosphorylation and activity opens up new possibilities for the development and testing of novel therapeutic strategies to control both proliferative and metastatic tumor growth.
format	article
author	Anup Shrestha Henrike Bruckmueller Hanne Kildalsen Gurjit Kaur Matthias Gaestel Hilde Ljones Wetting Ingvild Mikkola Ole-Morten Seternes
author_facet	Anup Shrestha Henrike Bruckmueller Hanne Kildalsen Gurjit Kaur Matthias Gaestel Hilde Ljones Wetting Ingvild Mikkola Ole-Morten Seternes
author_sort	Anup Shrestha
title	Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
title_short	Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
title_full	Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
title_fullStr	Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
title_full_unstemmed	Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription
title_sort	phosphorylation of steroid receptor coactivator-3 (src-3) at serine 857 is regulated by the p38mapk-mk2 axis and affects nf-κb-mediated transcription
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/0e455ff65b5a4346bcb8398d6c90b6fa
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Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38MAPK-MK2 axis and affects NF-κB-mediated transcription

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