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.
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Yuexin
Y
Xu
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Bing
B
Yao
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Kaikai
K
Shi
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Jianlei
J
Lu
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China.
Yucui
Y
Jin
Department of Oral Pathology, Affiliated Hospital of Stomatology, Nanjing Medical University, Hanzhong Road 136, Nanjing 210029, P.R. China.
Bing
B
Qi
Department of Oral and Maxillofacial Surgery, Affiliated Hospital of Stomatology, Nanjing Medical University, Hanzhong Road 136, Nanjing 210029, P.R. China.
Hongwei
H
Li
Department of Laboratory Medicine, The First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, P.R. China.
Shiyang
S
Pan
Molecular Endocrinology Laboratory, Department of Endocrinology, Odense University Hospital, Winslowparken 25. Sal 1, DK-5000 Odense C, Denmark.
Li
L
Chen
Department of Developmental Genetics, Nanjing Medical University, Hanzhong Road 140, Nanjing 210029, P.R. China. Electronic address: cyma@njmu.edu.cn.
Changyan
C
Ma
D000818:Animals; D002460:Cell Line; D005786:Gene Expression Regulation; D038362:Glycogen Synthase Kinase 3 / Q000378:metabolism*; D000071679:Glycogen Synthase Kinase 3 beta; D057809:HEK293 Cells; D006801:Humans; D051379:Mice; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D055550:Protein Stability; D012694:Serine / Q000378:metabolism*; D000076182:Sp7 Transcription Factor; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*
D000076182:Sp7 Transcription Factor; C478163:SP7 protein, human; C479466:Sp7 protein, mouse; D014157:Transcription Factors; D012694:Serine; C000605506:GSK3B protein, human; D000071679:Glycogen Synthase Kinase 3 beta; C000605507:Gsk3b protein, mouse; D038362:Glycogen Synthase Kinase 3
Mass spectrometric analysis; Osteoblast differentiation; Osterix; Phosphorylation modification; Protein stability; Transactivation activity