Abstract
Osterix is an osteoblast-specific transcriptional factor that is essential for osteoblast differentiation and bone formation. Calcineurin regulates bone formation through modulating osteoblast differentiation. However, post-translational modification of osterix such as phosphorylation and interactions between osterix and calcineurin remains unclear. In the present study, we demonstrated that calcineurin interacted with osterix determined by immunoprecipitation assay and Western analysis. Immunocytochemical study also revealed that osterix and calcineurin were co-localized in nucleus. Deletion of calcineurin binding motif on osterix molecule disrupted osterix-calcineurin interaction. Phosphorylation status of osterix was augmented by treatment with phosphatase inhibitors, FK506 and calyculin A. In contrast, treatment of recombinant calcineurin reduced phosphorylation status of osterix. Our present study suggests that calcineurin has an important role in the function of osterix through its modification of phosphorylation.
| Original language | English |
|---|---|
| Pages (from-to) | 440-444 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 379 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 6 2009 |
| Externally published | Yes |
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Keywords
- Calcineurin
- Osterix
- Phosphorylation
- Protein-protein interaction
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
Calcineurin regulates phosphorylation status of transcription factor osterix. / Okamura, Hirohiko; Amorim, Bruna Rabelo; Wang, Jie; Yoshida, Kaya; Haneji, Tatsuji.
In: Biochemical and Biophysical Research Communications, Vol. 379, No. 2, 06.02.2009, p. 440-444.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Calcineurin regulates phosphorylation status of transcription factor osterix
AU - Okamura, Hirohiko
AU - Amorim, Bruna Rabelo
AU - Wang, Jie
AU - Yoshida, Kaya
AU - Haneji, Tatsuji
PY - 2009/2/6
Y1 - 2009/2/6
N2 - Osterix is an osteoblast-specific transcriptional factor that is essential for osteoblast differentiation and bone formation. Calcineurin regulates bone formation through modulating osteoblast differentiation. However, post-translational modification of osterix such as phosphorylation and interactions between osterix and calcineurin remains unclear. In the present study, we demonstrated that calcineurin interacted with osterix determined by immunoprecipitation assay and Western analysis. Immunocytochemical study also revealed that osterix and calcineurin were co-localized in nucleus. Deletion of calcineurin binding motif on osterix molecule disrupted osterix-calcineurin interaction. Phosphorylation status of osterix was augmented by treatment with phosphatase inhibitors, FK506 and calyculin A. In contrast, treatment of recombinant calcineurin reduced phosphorylation status of osterix. Our present study suggests that calcineurin has an important role in the function of osterix through its modification of phosphorylation.
AB - Osterix is an osteoblast-specific transcriptional factor that is essential for osteoblast differentiation and bone formation. Calcineurin regulates bone formation through modulating osteoblast differentiation. However, post-translational modification of osterix such as phosphorylation and interactions between osterix and calcineurin remains unclear. In the present study, we demonstrated that calcineurin interacted with osterix determined by immunoprecipitation assay and Western analysis. Immunocytochemical study also revealed that osterix and calcineurin were co-localized in nucleus. Deletion of calcineurin binding motif on osterix molecule disrupted osterix-calcineurin interaction. Phosphorylation status of osterix was augmented by treatment with phosphatase inhibitors, FK506 and calyculin A. In contrast, treatment of recombinant calcineurin reduced phosphorylation status of osterix. Our present study suggests that calcineurin has an important role in the function of osterix through its modification of phosphorylation.
KW - Calcineurin
KW - Osterix
KW - Phosphorylation
KW - Protein-protein interaction
UR - http://www.scopus.com/inward/record.url?scp=58149517229&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=58149517229&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2008.12.094
DO - 10.1016/j.bbrc.2008.12.094
M3 - Article
C2 - 19114031
AN - SCOPUS:58149517229
VL - 379
SP - 440
EP - 444
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -