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Src enhances osteogenic differentiation through phosphorylation of Osterix.

Abstract：

:Osterix, a zinc-finger transcription factor, is required for osteoblast differentiation and new bone formation during embryonic development. The c-Src of tyrosine kinase is involved in a variety of cellular signaling pathways, leading to the induction of DNA synthesis, cell proliferation, and cytoskeletal reorganization. Src activity is tightly regulated and its dysregulation leads to constitutive activation and cellular transformation. The function of Osterix can be also modulated by post-translational modification. But the precise molecular signaling mechanisms between Osterix and c-Src are not known. In this study we investigated the potential regulation of Osterix function by c-Src in osteoblast differentiation. We found that c-Src activation increases protein stability, osteogenic activity and transcriptional activity of Osterix. The siRNA-mediated knockdown of c-Src decreased the protein levels and transcriptional activity of Osterix. Conversely, Src specific inhibitor, SU6656, decreased the protein levels and transcriptional activity of Osterix. The c-Src interacts with and phosphorylates Osterix. These results suggest that c-Src signaling modulates osteoblast differentiation at least in part through Osterix.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

Choi YH,Han Y,Lee SH,Cheong H,Chun KH,Yeo CY,Lee KY

doi

10.1016/j.mce.2015.03.010

subject

Has Abstract

pub_date

2015-05-15 00:00:00

pages

85-97

eissn

0303-7207

issn

1872-8057

pii

S0303-7207(15)00141-0

journal_volume

407

pub_type

杂志文章

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