Protein kinase A phosphorylates and regulates the osteogenic activity of Dlx5

Younho Han; Yun Hye Jin; Jinah Yum; Hyung Min Jeong; Joong Kook Choi; Chang Yeol Yeo; Kwang Youl Lee

doi:10.1016/j.bbrc.2011.03.034

Protein kinase A phosphorylates and regulates the osteogenic activity of Dlx5

Younho Han, Yun Hye Jin, Jinah Yum, Hyung Min Jeong, Joong Kook Choi, Chang Yeol Yeo, Kwang Youl Lee

Department of Life Science

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

8 Scopus citations

Abstract

Dlx5 transcription factor plays important roles in osteoblast differentiation and its transcription is regulated by many osteogenic signals including BMP-2. Recent studies suggest that the function of Dlx5 is also regulated post-translationally by protein kinases such as p38 and CaMKII. Protein kinase A (PKA) is involved in several steps of osteoblast differentiation and its activity has been shown necessary, yet not sufficient, for BMP-induced osteoblast differentiation. PKA is a ubiquitous cellular kinase that phosphorylates serine and threonine residues(s) of target proteins. In this study, we investigated the potential regulation of Dlx5 function by PKA in osteoblast differentiation. We found that PKA phosphorylates Dlx5 and that PKA activation increases the protein stability, osteogenic activity and transcriptional activity of Dlx5. We also found that BMP-2 increases the protein level of Dlx5 in a PKA activity-dependent manner. These results suggest that PKA activity enhances the osteogenic function of Dlx5, at least in part, through protein stabilization and that BMP-2 regulates the osteogenic function of Dlx5, at least in part, through PKA.

Original language	English
Pages (from-to)	461-465
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	407
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2011.03.034
State	Published - 15 Apr 2011

Bibliographical note

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

Keywords

BMP-2
Dlx5
Osteoblast differentiation
Protein kinase A

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10.1016/j.bbrc.2011.03.034

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title = "Protein kinase A phosphorylates and regulates the osteogenic activity of Dlx5",

abstract = "Dlx5 transcription factor plays important roles in osteoblast differentiation and its transcription is regulated by many osteogenic signals including BMP-2. Recent studies suggest that the function of Dlx5 is also regulated post-translationally by protein kinases such as p38 and CaMKII. Protein kinase A (PKA) is involved in several steps of osteoblast differentiation and its activity has been shown necessary, yet not sufficient, for BMP-induced osteoblast differentiation. PKA is a ubiquitous cellular kinase that phosphorylates serine and threonine residues(s) of target proteins. In this study, we investigated the potential regulation of Dlx5 function by PKA in osteoblast differentiation. We found that PKA phosphorylates Dlx5 and that PKA activation increases the protein stability, osteogenic activity and transcriptional activity of Dlx5. We also found that BMP-2 increases the protein level of Dlx5 in a PKA activity-dependent manner. These results suggest that PKA activity enhances the osteogenic function of Dlx5, at least in part, through protein stabilization and that BMP-2 regulates the osteogenic function of Dlx5, at least in part, through PKA.",

keywords = "BMP-2, Dlx5, Osteoblast differentiation, Protein kinase A",

author = "Younho Han and Jin, {Yun Hye} and Jinah Yum and Jeong, {Hyung Min} and Choi, {Joong Kook} and Yeo, {Chang Yeol} and Lee, {Kwang Youl}",

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

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AU - Choi, Joong Kook

AU - Yeo, Chang Yeol

AU - Lee, Kwang Youl

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N2 - Dlx5 transcription factor plays important roles in osteoblast differentiation and its transcription is regulated by many osteogenic signals including BMP-2. Recent studies suggest that the function of Dlx5 is also regulated post-translationally by protein kinases such as p38 and CaMKII. Protein kinase A (PKA) is involved in several steps of osteoblast differentiation and its activity has been shown necessary, yet not sufficient, for BMP-induced osteoblast differentiation. PKA is a ubiquitous cellular kinase that phosphorylates serine and threonine residues(s) of target proteins. In this study, we investigated the potential regulation of Dlx5 function by PKA in osteoblast differentiation. We found that PKA phosphorylates Dlx5 and that PKA activation increases the protein stability, osteogenic activity and transcriptional activity of Dlx5. We also found that BMP-2 increases the protein level of Dlx5 in a PKA activity-dependent manner. These results suggest that PKA activity enhances the osteogenic function of Dlx5, at least in part, through protein stabilization and that BMP-2 regulates the osteogenic function of Dlx5, at least in part, through PKA.

AB - Dlx5 transcription factor plays important roles in osteoblast differentiation and its transcription is regulated by many osteogenic signals including BMP-2. Recent studies suggest that the function of Dlx5 is also regulated post-translationally by protein kinases such as p38 and CaMKII. Protein kinase A (PKA) is involved in several steps of osteoblast differentiation and its activity has been shown necessary, yet not sufficient, for BMP-induced osteoblast differentiation. PKA is a ubiquitous cellular kinase that phosphorylates serine and threonine residues(s) of target proteins. In this study, we investigated the potential regulation of Dlx5 function by PKA in osteoblast differentiation. We found that PKA phosphorylates Dlx5 and that PKA activation increases the protein stability, osteogenic activity and transcriptional activity of Dlx5. We also found that BMP-2 increases the protein level of Dlx5 in a PKA activity-dependent manner. These results suggest that PKA activity enhances the osteogenic function of Dlx5, at least in part, through protein stabilization and that BMP-2 regulates the osteogenic function of Dlx5, at least in part, through PKA.

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Protein kinase A phosphorylates and regulates the osteogenic activity of Dlx5

Abstract

Bibliographical note

Keywords

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