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Updated: Apr 16, 2026

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
Published on: April 1, 2022
Phosphorylation of Serine422 increases the stability and transactivation activities of human Osterix
Yuexin Xu1, Bing Yao1, Kaikai Shi1
1Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Abstract:
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.
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