NFATc1 phosphorylation by DYRK1A increases its protein stability.

NFATc1 phosphorylation by DYRK1A increases its protein stability.

NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional ac...

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Main Authors: Heng Liu, Ketao Wang, Shuai Chen, Qian Sun, Yuankai Zhang, Long Chen, Xiulian Sun
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5325557?pdf=render
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spelling doaj-09445d6f73cc413294313aad235903d42020-11-25T00:08:53ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01122e017298510.1371/journal.pone.0172985NFATc1 phosphorylation by DYRK1A increases its protein stability.Heng LiuKetao WangShuai ChenQian SunYuankai ZhangLong ChenXiulian SunNFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1.http://europepmc.org/articles/PMC5325557?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Heng Liu
Ketao Wang
Shuai Chen
Qian Sun
Yuankai Zhang
Long Chen
Xiulian Sun
spellingShingle Heng Liu
Ketao Wang
Shuai Chen
Qian Sun
Yuankai Zhang
Long Chen
Xiulian Sun
NFATc1 phosphorylation by DYRK1A increases its protein stability.
PLoS ONE
author_facet Heng Liu
Ketao Wang
Shuai Chen
Qian Sun
Yuankai Zhang
Long Chen
Xiulian Sun
author_sort Heng Liu
title NFATc1 phosphorylation by DYRK1A increases its protein stability.
title_short NFATc1 phosphorylation by DYRK1A increases its protein stability.
title_full NFATc1 phosphorylation by DYRK1A increases its protein stability.
title_fullStr NFATc1 phosphorylation by DYRK1A increases its protein stability.
title_full_unstemmed NFATc1 phosphorylation by DYRK1A increases its protein stability.
title_sort nfatc1 phosphorylation by dyrk1a increases its protein stability.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2017-01-01
description NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1.
url http://europepmc.org/articles/PMC5325557?pdf=render
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