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

doi:10.1016/j.bbrc.2011.05.064

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

Department of Life Science

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

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 language	English
Pages (from-to)	681-686
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	409
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2011.05.064
State	Published - 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.

Keywords

Akt
Bone formation
Dlx5
Protein stability

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10.1016/j.bbrc.2011.05.064

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title = "Akt phosphorylates and regulates the function of Dlx5",

abstract = "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.",

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author = "Jeong, {Hyung Min} and Jin, {Yun Hye} and Kim, {Yeon Jin} and Jinah Yum and Choi, {You Hee} and Yeo, {Chang Yeol} and Lee, {Kwang Youl}",

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.",

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AU - Jeong, Hyung Min

AU - Jin, Yun Hye

AU - Kim, Yeon Jin

AU - Yum, Jinah

AU - Choi, You Hee

AU - Yeo, Chang Yeol

AU - Lee, Kwang Youl

N1 - 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.

PY - 2011/6/17

Y1 - 2011/6/17

N2 - 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.

AB - 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.

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Akt phosphorylates and regulates the function of Dlx5

Abstract

Bibliographical note

Keywords

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