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Author Meng, Rui ♦ Al Quobaili, Faizeh ♦ Müller, Isabelle ♦ Götz, Claudia ♦ Thiel, Gerald ♦ Montenarh, Mathias
Source SpringerLink
Content type Text
Publisher SP Birkhäuser Verlag Basel
File Format PDF
Copyright Year ©2010
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology
Subject Keyword Protein kinase ♦ Phosphorylation ♦ Transcription factor ♦ Homeobox protein ♦ Insulin production ♦ Biochemistry ♦ Life Sciences ♦ Biomedicine general ♦ Cell Biology
Abstract The duodenal homeobox-1 protein Pdx-1 is one of the regulators for the transcription of the insulin gene. Pdx-1 is a phosphoprotein, and there is increasing evidence for the regulation of some of its functions by phosphorylation. Here, we asked whether protein kinase CK2 might phosphorylate Pdx-1 and how this phosphorylation could be implicated in the functional regulation of Pdx-1. We used fragments of Pdx-1 as well as phosphorylation mutants for experiments with protein kinase CK2. Transactivation was measured by reporter assays using the insulin promoter. Our data showed that Pdx-1 is phosphorylated by protein kinase CK2 at amino acids thr231 and ser232, and this phosphorylation was implicated in the regulation of the transcription factor activity of Pdx-1. Furthermore, inhibition of protein kinase CK2 by specific inhibitors led to an elevated release of insulin from pancreatic β-cells. Thus, these findings identify CK2 as a novel mediator of the insulin metabolism.
ISSN 1420682X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2010-03-26
Publisher Place Basel
e-ISSN 14209071
Journal Cellular and Molecular Life Sciences
Volume Number 67
Issue Number 14
Page Count 9
Starting Page 2481
Ending Page 2489

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Source: SpringerLink