Protein Kinase A Phosphorylates Dlx3 and Regulates the Function of Dlx3 During Osteoblast Differentiation

Title
Protein Kinase A Phosphorylates Dlx3 and Regulates the Function of Dlx3 During Osteoblast Differentiation
Author(s)
정태천Li H[Li H]정형민[정형민]최유희[최유희]김주희[김주희]최중국[최중국]여창열[여창열]정혜광[정혜광]천창주[천창주]이광열[이광열]
Keywords
BONE MORPHOGENETIC PROTEINS; VASCULAR CELLS; DISTINCT ROLES; ACTIVATION; EXPRESSION; PKA; PATHWAY; GENES; RUNX2; CALCIFICATION
Issue Date
201411
Publisher
WILEY-BLACKWELL
Citation
JOURNAL OF CELLULAR BIOCHEMISTRY, v.115, no.11, pp.2004 - 2011
Abstract
Protein kinase A (PKA), a serine/threonine kinase, regulates bone formation, and enhances Bone morphogenetic protein (BMP)-induced osteoblast differentiation. However, the mechanisms of how PKA controls the cellular response to BMP are not well known. We investigated the effects of modulating PKA activity during BMP2-induced osteoblast differentiation, and found that PKA regulates the function of Dlx3. Dlx3 plays crucial roles in osteoblast differentiation and it is expressed in most skeletal elements during development. We found that PKA activation increases BMP2-induced expression of Dlx3 protein, and enhances the protein stability, DNA binding, and transcriptional activity of Dlx3. In addition, PKA activation induces the phosphorylation of Dlx3 at consensus PKA phosphorylation target site(s). Lastly, substitution of serine 10 in Dlx3 to alanine significantly reduces, if not completely abolishes, the phosphorylation of Dlx3 and the regulation of Dlx3 function by PKA. These results suggest that Dlx3 is a novel target of PKA, and that PKA mediates BMP signaling during osteoblast differentiation, at least in part, by phosphorylating Dlx3 and modulating the protein stability and function of Dlx3. J. Cell. Biochem. 115: 2004-2011, 2014. (c) 2014 Wiley Periodicals, Inc.
URI
http://hdl.handle.net/YU.REPOSITORY/30488http://dx.doi.org/10.1002/jcb.24872
ISSN
0730-2312
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약학대학 > 약학부 > Articles
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