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CK2 phosphorylation of C/EBPδ regulates its transcription factor activity

Lisa Schwind1, Andreas D Zimmer1, Claudia Götz1

  • 1Medical Biochemistry and Molecular Biology, Saarland University, Building 44, D-66424 Homburg, Germany.

The International Journal of Biochemistry & Cell Biology
|February 15, 2015
PubMed

Insights

Protein kinase CK2 phosphorylates CCAAT/enhancer binding protein δ (C/EBPδ), a key transcription factor. This phosphorylation modulates C/EBPδ

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein kinase CK2 is a crucial regulator of cell viability.
  • CK2 phosphorylates numerous cellular targets, including transcription factors.
  • CCAAT/enhancer binding protein δ (C/EBPδ) is involved in cellular processes.

Purpose of the Study:

  • To identify new substrates for protein kinase CK2.
  • To investigate the role of CK2 in regulating C/EBPδ function.

Main Methods:

  • Site-directed mutagenesis to identify phosphorylation sites.
  • Western blotting and co-immunoprecipitation to assess protein interactions and localization.
  • Reporter assays to measure transcriptional activity.

Main Results:

  • C/EBPδ was identified as a novel substrate for CK2.
  • Serine 57 in the transactivation domain was mapped as the major CK2 phosphorylation site.
  • CK2 phosphorylation of C/EBPδ modulates its transcriptional activity without affecting localization or C/EBPβ interaction.

Conclusions:

  • CK2 phosphorylation regulates the transcriptional activity of C/EBPδ.
  • CK2 may target the transcriptional machinery through its interaction with C/EBPδ.
Keywords:
PhosphorylationProtein kinase CK2Protein–protein interactionTranscriptionTranscription factor

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