Akt phosphorylates and regulates the osteogenic activity of Osterix

You Hee Choi, Hyung Min Jeong, Yun Hye Jin, Hongyan Li, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


Osterix (Osx), a zinc-finger transcription factor is required for osteoblast differentiation and new bone formation during embryonic development. Akt is a member of the serine/threonine-specific protein kinase and plays important roles in osteoblast differentiation. The function of Osterix can be also modulated by post-translational modification. But, the precise molecular signaling mechanisms between Osterix and Akt are not known. In this study, we investigated the potential regulation of Osterix function by Akt in osteoblast differentiation. We found that Akt phosphorylates Osterix and that Akt activation increases protein stability, osteogenic activity and transcriptional activity of Osterix. We also found that BMP-2 increases the protein level of Osterix in an Akt activity-dependent manner. These results suggest that Akt activity enhances the osteogenic function of Osterix, at least in part, through protein stabilization and that BMP-2 regulates the osteogenic function of Osterix, at least in part, through Akt.

Original languageEnglish
Pages (from-to)637-641
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 5 Aug 2011

Bibliographical note

Funding Information:
This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 2010-0003279 ).


  • Akt
  • Bone formation
  • Osterix
  • Phosphorylation
  • Protein stability


Dive into the research topics of 'Akt phosphorylates and regulates the osteogenic activity of Osterix'. Together they form a unique fingerprint.

Cite this