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Cbl-b and c-Cbl negatively regulate osteoblast differentiation by enhancing ubiquitination and degradation of Osterix
- Cbl-b and c-Cbl negatively regulate osteoblast differentiation by enhancing ubiquitination and degradation of Osterix
- Choi, You Hee; Han, Younho; Lee, Sung Ho; Jin, Yun-Hye; Bahn, Minjin; Hur, Kyu Chung; Yeo, Chang-Yeol; Lee, Kwang Youl
- Ewha Authors
- 허규정; 여창열
- SCOPUS Author ID
- 허규정; 여창열
- Issue Date
- Journal Title
- 8756-3282; 1873-2763
- vol. 75, pp. 201 - 209
- Cbl; Osterix; Ubiquitination; Osteoblast differentiation
- ELSEVIER SCIENCE INC
- SCI; SCIE; SCOPUS
- E3 ubiquitin ligase Cbl-b and c-Cbl play important roles in bone formation and maintenance. Cbl-b and c-Cbl regulate the activity of various receptor tyrosine kinases and intracellular protein tyrosine kinases mainly by regulating the degradation of target proteins. However, the precise mechanisms of how Cbl-b and c-Cbl regulate osteoblast differentiation are not well known. In this study, we investigated potential targets of Cbl-b and c-Cbl. We found that Cbl-b and c-Cbl inhibit BMP2-induced osteoblast differentiation in mesenchymal cells. Among various osteogenic transcription factors, we identified that Cbl-b and c-Cbl suppress the protein stability and transcriptional activity of Osterix. Our results suggest that Cbl-b and c-Cbl inhibit the function of Osterix by enhancing the ubiquitin-proteasome-mediated degradation of Osterix. Taken together, we propose novel regulatory roles of Cbl-b and c-Cbl during osteoblast differentiation in which Cbl-b and c-Cbl regulate the degradation of Osterix through the ubiquitin-proteasome pathway. (C) 2015 Elsevier Inc. All rights reserved.
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