The stability of CREB3/Luman is regulated by protein kinase CK2 phosphorylation.

Beate Maria Schmitt, Emmanuel Ampofo, Heike Stumpf, Mathias Montenarh, Claudia Götz

Journal: Biochemical and biophysical research communications 2020;523(3):639-644

PMID: 31941600

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Abstract

CREB3 (Luman) is a family member of ER resident transcription factors, which are cleaved upon the induction of ER stress. Their N-terminal fragments shuttle into the nucleus where they regulate the transcription of target genes. Here, we found that human CREB3 is phosphorylated within its transcription activation domain on serine 46 by protein kinase CK2. Further analyses revealed that the phosphorylation of this site does neither affect the cleavage by S1P/S2P proteases, nor the nuclear localisation nor the transcriptional activity of CREB3. However, phosphorylation at serine 46 reduced the stability of CREB3.

Address: Institute for Clinical and Experimental Surgery, Saarland University, Building 65, 66424, Homburg, Germany.; Medical Biochemistry and Molecular Biology, Saarland University, Building 44, 66424, Homburg, Germany.; Medical Biochemistry and Molecular Biology, Saarland University, Building 44, 66424, Homburg, Germany. Electronic address: [email protected].

DOI: 10.1016/j.bbrc.2019.12.118

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MeSH Terms: Amino Acid Sequence, Casein Kinase II, Cyclic AMP Response Element-Binding Protein, HEK293 Cells, Humans, Phosphorylation, Protein Stability