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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Veröffentlicht in:	PloS one 2017-02, Vol.12 (2), p.e0172985-e0172985
Hauptverfasser:	Liu, Heng, Wang, Ketao, Chen, Shuai, Sun, Qian, Zhang, Yuankai, Chen, Long, Sun, Xiulian
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Analysis Biology and Life Sciences Cancer Cytoplasm Down syndrome Drosophila Dyrk Kinases Genetic aspects HEK293 Cells Humans Immune response Immunology Insects Kinases Lymphocytes Medicine and Health Sciences Monoclonal antibodies NFATC Transcription Factors - metabolism Otolaryngology Phosphorylation Physical Sciences Physiological aspects Proteasome Endopeptidase Complex - metabolism Proteasomes Protein expression Protein Serine-Threonine Kinases - metabolism Protein Stability Protein-Tyrosine Kinases - metabolism Proteins Proteolysis Research and Analysis Methods T cells Transcription factors Ubiquitin Ubiquitination
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Zusammenfassung:	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.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0172985