ArticleThe Journal of biological chemistry2010
p38 regulates expression of osteoblast-specific genes by phosphorylation of osterix.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 121 citations in OpenAlex.
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- The Role of Aryl Hydrocarbon Receptor in Bone Biology.International journal of tryptophan research : IJTR · 2024Review
- Tmem161a regulates bone formation and bone strength through the P38 MAPK pathway.Scientific reports · 2023Article
- NIR irradiation of human buccal fat pad adipose stem cells and its effect on TRP ion channels.Lasers in medical science · 2022Article
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- The role of Trithorax family regulating osteogenic and Chondrogenic differentiation in mesenchymal stem cells.Cell proliferation · 2022Review
- Transcriptomic Analysis Provides Insights to Reveal theFrontiers in cell and developmental biology · 2022Article
- miR-20a-5p contributes to osteogenic differentiation of human dental pulp stem cells by regulating BAMBI and activating the phosphorylation of Smad5 and p38.Stem cell research & therapy · 2021Article
- Targeted Ptpn11 deletion in mice reveals the essential role of SHP2 in osteoblast differentiation and skeletal homeostasis.Bone research · 2021Article
- Spatial-Temporal Patterns and Inflammatory Factors of Bone Matrix Remodeling.Stem cells international · 2021Review
- The effects of mineral trioxide aggregate on osteo/odontogenic potential of mesenchymal stem cells: a comprehensive and systematic literature review.Biomaterial investigations in dentistry · 2020Review
- Influence of the TGF-β Superfamily on Osteoclasts/Osteoblasts Balance in Physiological and Pathological Bone Conditions.International journal of molecular sciences · 2020Review
- The potential function of miR-135b-mediated JAK2/STAT3 signaling pathway during osteoblast differentiation.The Kaohsiung journal of medical sciences · 2020Article
- Metformin coordinates osteoblast/osteoclast differentiation associated with ischemic osteonecrosis.Aging · 2020Article
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- ATP-Dependent Chromatin Remodeling Complex in the Lineage Specification of Mesenchymal Stem Cells.Stem cells international · 2020Review
- An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling.F1000Research · 2020Review
- Recent Advances of Osterix Transcription Factor in Osteoblast Differentiation and Bone Formation.Frontiers in cell and developmental biology · 2020Review
1 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Osterix, a zinc finger transcription factor, is specifically expressed in osteoblasts and osteocytes of all developing bones. Because no bone formation occurs in Osx-null mice, Osterix is thought to be an essential regulator of osteoblast differentiation. We report that, in several mesenchymal and osteoblastic cell types, BMP-2 induces an increase in expression of the two isoforms of Osterix arising from two alternative promoters. We identified a consensus Sp1 sequence (GGGCGG) as Osterix binding regions in the fibromodulin and the bone sialoprotein promoters in vitro and in vivo. Furthermore, we show that Osterix is a novel substrate for p38 MAPK in vitro and in vivo and that Ser-73 and Ser-77 are the regulatory sites phosphorylated by p38. Our data also demonstrate that Osterix is able to increase recruitment of p300 and Brg1 to the promoters of its target genes fibromodulin and bone sialoprotein in vivo and that it directly associates with these cofactors through protein-protein interactions. Phosphorylation of Osterix at Ser-73/77 increased its ability to recruit p300 and SWI/SNF to either fibromodulin or bone sialoprotein promoters. We therefore propose that Osterix binds to Sp1 sequences on target gene promoters and that its phosphorylation by p38 enhances recruitment of coactivators to form transcriptionally active complexes.
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