NFATc1 phosphorylation by DYRK1A increases its protein stability.
NFATc1 phosphorylation by DYRK1A increases its protein stability.
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DOI:
10.1371/journal.pone.0172985
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发表时间:
2017
期刊:
影响因子:
3.7
通讯作者:
Sun X
中科院分区:
文献类型:
--
作者:
Liu H;Wang K;Chen S;Sun Q;Zhang Y;Chen L;Sun X
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.