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

Authors :
Takai, Tomoko
Matsuda, Tomokazu
Matsuura, Yuki
Inoue, Kaho
Suzuki, Emi
Kanno, Ayumi
Kimura-Koyanagi, Maki
Asahara, Shun-ichiro
Hatano, Naoya
Ogawa, Wataru
Kido, Yoshiaki
Source :
Biochemical & Biophysical Research Communications. Feb2018, Vol. 497 Issue 1, p451-456. 6p.
Publication Year :
2018

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0006291X
Volume :
497
Issue :
1
Database :
Academic Search Index
Journal :
Biochemical & Biophysical Research Communications
Publication Type :
Academic Journal
Accession number :
128226376
Full Text :
https://doi.org/10.1016/j.bbrc.2018.02.108