Open AccessNFATc1 phosphorylation by DYRK1A increases its protein stability
Author(s) -
Heng Liu,
Ketao Wang,
Shuai Chen,
Qian Sun,
Yuankai Zhang,
Long Chen,
Xiulian Sun
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0172985
Subject(s) - dyrk1a , phosphorylation , ubiquitin , kinase , proteasome , transcription factor , transcription (linguistics) , protein kinase a , chemistry , microbiology and biotechnology , biology , biochemistry , gene , linguistics , philosophy
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/α A protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/α A 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.