Phosphorylation of Serine422 increases the stability and transactivation activities of human Osterix.
Osterix (Osx) is an essential regulator for osteoblast differentiation and bone formation. Although phosphorylation has been reported to be involved in the regulation of Osx activity, the precise underlying mechanisms remain to be elucidated. Here we identified S422 as a novel phosphorylation site of Osx and demonstrated that GSK-3β interacted ... and co-localized with Osx. GSK-3β increased the stability and transactivation activity of Osx through phosphorylation of the newly identified site. These findings expanded our understanding of the mechanisms of posttranslational regulation of Osx and the role of GSK-3β in the control of Osx transactivation activity.
Mesh Terms:
Animals, Cell Line, Gene Expression Regulation, Glycogen Synthase Kinase 3, HEK293 Cells, Humans, Mice, Mutagenesis, Site-Directed, Phosphorylation, Protein Stability, Serine, Transcription Factors
Animals, Cell Line, Gene Expression Regulation, Glycogen Synthase Kinase 3, HEK293 Cells, Humans, Mice, Mutagenesis, Site-Directed, Phosphorylation, Protein Stability, Serine, Transcription Factors
FEBS Lett.
Date: Mar. 24, 2015
PubMed ID: 25728276
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