NFATc1 phosphorylation by DYRK1A increases its protein stability.

NFATc1 phosphorylation by DYRK1A increases its protein stability.
复制标题

DOI:
10.1371/journal.pone.0172985
复制
发表时间:
2017
期刊:
影响因子:
3.7
通讯作者:
Sun X
Sun X
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Liu H;Wang K;Chen S;Sun Q;Zhang Y;Chen L;Sun X

文献摘要

被引文献

相似文献

NFAT是参与免疫激活和肿瘤进展的转录因子。先前的报道显示DYRK 1A通过磷酸化抑制NFATc 2的转录活性。尽管如此,我们的研究结果表明,DYRK 1A增加NFATc 1/αA蛋白水平和随后的转录活性。NFATc 1/αA在S261、S278、S403和S409处的DYRK 1A磷酸化干扰NFATc 1泛素化和泛素-蛋白酶体降解。我们的研究结果表明,DYRK 1A是一个积极的激酶调节NFATc 1。
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.