NFATc1 phosphorylation by DYRK1A increases its protein stability.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28235034.
- Also identified by DOI 10.1371/journal.pone.0172985 and PMC identifier 5325557.
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Abstract
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.
Medical subject headings
- NFATC Transcription Factors
- Protein Serine-Threonine Kinases
- Protein-Tyrosine Kinases
- Ubiquitination