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.
| Original language | English |
|---|---|
| Pages (from-to) | 451-456 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 497 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Feb 26 2018 |
| Externally published | Yes |
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Keywords
- Casein kinase 2 (CK2)
- CCAAT/Enhancer-binding protein β (C/EBPβ)
- Endoplasmic reticulum stress
- Pancreatic β cell failure
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Casein kinase 2 phosphorylates and stabilizes C/EBPβ in pancreatic β cells. / Takai, Tomoko; Matsuda, Tomokazu; Matsuura, Yuki; Inoue, Kaho; Suzuki, Emi; Kanno, Ayumi; Kimura-Koyanagi, Maki; Asahara, Shun ichiro; Hatano, Naoya; Ogawa, Wataru; Kido, Yoshiaki.
In: Biochemical and Biophysical Research Communications, Vol. 497, No. 1, 26.02.2018, p. 451-456.Research output: Contribution to journal › Article
}
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
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 - Casein kinase 2 (CK2)
KW - CCAAT/Enhancer-binding protein β (C/EBPβ)
KW - Endoplasmic reticulum stress
KW - Pancreatic β cell failure
UR - http://www.scopus.com/inward/record.url?scp=85042039276&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85042039276&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2018.02.108
DO - 10.1016/j.bbrc.2018.02.108
M3 - Article
VL - 497
SP - 451
EP - 456
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -