Akt phosphorylates and regulates the function of Dlx5

Hyung Min Jeong, Yun Hye Jin, Yeon Jin Kim, Jinah Yum, You Hee Choi, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Akt, a phosphoinositide-dependent serine/threonine protein kinase, acts as a key regulator in bone formation. Akt can be activated by several osteogenic signaling molecules, but its precise function and downstream targets in bone development are unknown. Dlx5 transcription factor plays important roles during bone development and osteoblast differentiation. Its expression is regulated by several osteogenic signals. In addition, Dlx5 function is also regulated through post-translational modification by several kinases. In this report, we have investigated a potential regulation of Dlx5 function by Akt. Our results indicate that Akt interacts with and phosphorylates Dlx5. In addition, we provide evidences that Akt kinase activity is important for Akt to enhance the protein stability and transcriptional activity of Dlx5. These results suggest that Dlx5 is a novel target of Akt and that the activity of Dlx5 could be modulated by a novel mechanism involving Akt during osteoblast differentiation.

Original languageEnglish
Pages (from-to)681-686
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 17 Jun 2011

Bibliographical note

Funding Information:
This work was supported by the Korea Research Foundation of Korea Grant funded by the Korean Government to Y.-H. Jin ( MOEHRD, Basic Research Promotion Fund , KRF-2008-532-E00030 and NRF-2009-353-E00037 ) and C.-Y. Yeo ( KRF-2008-314-C00306 ). J. Yum is supported by the second stage of the Brain Korea 21 project.


  • Akt
  • Bone formation
  • Dlx5
  • Protein stability


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