Casein kinase 2 phosphorylates and stabilizes C/EBPβ in pancreatic β cells

Tomoko Takai, Tomokazu Matsuda, Yuki Matsuura, Kaho Inoue, Emi Suzuki, Ayumi Kanno, Maki Kimura-Koyanagi, Shun ichiro Asahara, Naoya Hatano, Wataru Ogawa, Yoshiaki Kido

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


During the development of type 2 diabetes, endoplasmic reticulum (ER) stress leads to pancreatic β cell failure. CCAAT/enhancer-binding protein (C/EBP) β is highly induced by ER stress and AMP-activated protein kinase (AMPK) suppression in pancreatic β cells, and its accumulation reduces pancreatic β cell mass. We investigated the phosphorylation state of C/EBPβ under these conditions. Casein kinase 2 (CK2) was found to co-localize with C/EBPβ in MIN6 cells. It phosphorylated S222 of C/EBPβ a previously unidentified phosphorylation site. We found that C/EBPβ is phosphorylated by CK2 under AMPK suppression and ER stress, which are important from the viewpoint of the worsening pathological condition of type 2 diabetes, such as decreased insulin secretion and apoptosis of pancreatic β cells.

Original languageEnglish
Pages (from-to)451-456
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Feb 26 2018
Externally publishedYes


  • CCAAT/Enhancer-binding protein β (C/EBPβ)
  • Casein kinase 2 (CK2)
  • Endoplasmic reticulum stress
  • Pancreatic β cell failure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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