Transcriptional regulation, of dentin matrix protein 1 by JunB and p300 during osteoblast differentiation

Karthikeyan Narayanan, Rampalli Srinivas, Mathew Craig Peterson, Amsaveni Ramachandran, Jianjun Hao, Bayar Thimmapaya, Philipp E. Scherer, Anne George*

*Corresponding author for this work

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

Dentin matrix protein 1 (DMP1) is an acidic noncollagenous protein localized specifically in the mineralized matrix of bone and dentin. Expression analyses demonstrate that DMP1 is differentially regulated in osteoblasts and odontoblasts. Earlier we have reported on the transcriptional regulation of DMP1 by c-Fos and c-Jun (AP-1) transcription factors. Results from earlier study indicate that c-Fos and c-Jun play an important role in early osteoblast differentiation, whereas they do not have a significant effect on the terminally differentiated osteoblasts. In this paper, we demonstrate a regulatory mechanism by which JunB transcriptionally controls the expression of DMP1 during osteoblast differentiation. The cooperative interaction of JunB with p300 has been shown to dramatically modulate the DMP1 promoter activity during mineralization. Immunoprecipitation and chromatin immunoprecipitation analysis demonstrate the interaction of JunB and p300 in vivo. Further, phosphorylation of JunB at Ser-79 was found to be essential for its interaction with p300. Intrinsic histone acetyltransferase activity of p300 also plays a critical role in regulating DMP1 gene expression.

Original languageEnglish (US)
Pages (from-to)44294-44302
Number of pages9
JournalJournal of Biological Chemistry
Volume279
Issue number43
DOIs
StatePublished - Oct 22 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Narayanan, K., Srinivas, R., Peterson, M. C., Ramachandran, A., Hao, J., Thimmapaya, B., Scherer, P. E., & George, A. (2004). Transcriptional regulation, of dentin matrix protein 1 by JunB and p300 during osteoblast differentiation. Journal of Biological Chemistry, 279(43), 44294-44302. https://doi.org/10.1074/jbc.M403511200