TY - JOUR
T1 - Casein kinase 2 phosphorylates and stabilizes C/EBPβ in pancreatic β cells
AU - Takai, Tomoko
AU - Matsuda, Tomokazu
AU - Matsuura, Yuki
AU - Inoue, Kaho
AU - Suzuki, Emi
AU - Kanno, Ayumi
AU - Kimura-Koyanagi, Maki
AU - Asahara, Shun ichiro
AU - Hatano, Naoya
AU - Ogawa, Wataru
AU - Kido, Yoshiaki
N1 - Funding Information:
This work was supported by a Grant-in-Aid for Scientific Research from the Japanese Ministry of Education, Culture, Sports, Science and Technology (MEXT; 17H01966 to YK); a Grant-in-Aid for Scientific Research from MEXT ( 17K09882 to SA); a Grant-in-Aid for Scientific Research from MEXT ( 20570344 to TM), and a Junior Scientist Development Grant supported by Novo Nordisk Pharma Ltd . to TM The funding sources had no role in the collection, analysis, and interpretation of data, in the writing of the report, and in the decision to submit the article for publication. Appendix A
Publisher Copyright:
© 2018 Elsevier Inc.
PY - 2018/2/26
Y1 - 2018/2/26
N2 - 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.
AB - 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.
KW - CCAAT/Enhancer-binding protein β (C/EBPβ)
KW - Casein kinase 2 (CK2)
KW - Endoplasmic reticulum stress
KW - Pancreatic β cell failure
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U2 - 10.1016/j.bbrc.2018.02.108
DO - 10.1016/j.bbrc.2018.02.108
M3 - Article
C2 - 29448105
AN - SCOPUS:85042039276
VL - 497
SP - 451
EP - 456
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -
