Helicobacter pylori Suppresses Glycogen Synthase Kinase 3β to Promote β-Catenin Activity

Olga Sokolova,Przemyslaw M Bozko,Michael Naumann

doi:10.1074/jbc.m801818200

Olga Sokolova, Przemyslaw M Bozko + Show 1 more

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https://doi.org/10.1074/jbc.m801818200

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Abstract

Helicobacter pylori Suppresses Glycogen Synthase Kinase 3β to Promote β-Catenin Activity

Highlights

␤-Catenin is a multifunctional protein that (i) participates in cell adhesion by bridging E-cadherin to ␣-catenin and (ii) mediates transcriptional regulation by forming a complex with LEF/ TCF2 transcription factors [11, 12]. ␤-Catenin redistribution in
We report that 1) H. pylori suppresses GSK3␤ activity in a CagA-independent manner, 2) H. pylori-induced suppression of GSK3␤ leads to inhibition of Ser/Thr phosphorylation, ubiquitinylation, and degradation of ␤-catenin, and 3) H. pylori stimulates ␤-catenin-dependent lymphoid enhancer-binding factor/T cell factor (LEF/TCF) transactivation activity and causes up-regulation of cyclin D1
LEF/TCF transcription factors are known to bind to cyclin D1 promoter and regulate gene expression [20]

Summary

Introduction

␤-Catenin is a multifunctional protein that (i) participates in cell adhesion by bridging E-cadherin to ␣-catenin and (ii) mediates transcriptional regulation by forming a complex with LEF/ TCF2 transcription factors [11, 12]. ␤-Catenin redistribution in. We report that 1) H. pylori suppresses GSK3␤ activity in a CagA-independent manner, 2) H. pylori-induced suppression of GSK3␤ leads to inhibition of Ser/Thr phosphorylation, ubiquitinylation, and degradation of ␤-catenin, and 3) H. pylori stimulates ␤-catenin-dependent LEF/TCF transactivation activity and causes up-regulation of cyclin D1. H. pylori stimulates ␤-catenin-dependent LEF/TCF transactivation activity and causes an increase of cyclin D1 level in MDCK cells.

Results

Conclusion