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

doi:10.1016/j.bbrc.2018.02.108

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 journal › Article › peer-review

1 Citation (Scopus)

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	https://doi.org/10.1016/j.bbrc.2018.02.108
Publication status	Published - Feb 26 2018
Externally published	Yes

Keywords

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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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 › peer-review

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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.",

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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

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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.

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