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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Eberspaecher, Heidi Yasuda, Hideyo Kishino, Tetsuya De Crombrugghe, Benoit Takigawa, Masaharu Maki, Sayumi Stephen, Shelley Hattori, Takako |
| Description | Author Affiliation: Hattori T ( From the Department of Biochemistry and Molecular Dentistry, Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama University, 2-5-1 Shikata-cho, Kita-ku Okayama 700-8525, Japan.) |
| Abstract | SOX9 is a transcription factor that acts as a key regulator at various stages of cartilage differentiation. There is ample evidence that intracellular SOX9 protein levels are tightly regulated both by sumoylation and by degradation through the ubiquitin-proteasome pathway. Using a proteomics approach, here we report the identification of a SOX9-binding protein, E6-AP/UBE3A, that may act as a ubiquitin ligase toward Sox9. E6-AP bound SOX9 through the region consisting mostly of its high mobility group domain in vitro. In nuclear lysates, FLAG-tagged E6-AP coprecipitated with Sox9 and its high mobility group domain. This finding was estimated using nuclear lysates from a chondrocytic cell line that endogenously expresses E6-AP and SOX9. Accordingly, ectopically expressed E6-AP and SOX9 colocalized in the nucleus. We show that E6-AP ubiquitinates SOX9 in vitro and in vivo and that SOX9 levels are enhanced after addition of the proteasome inhibitor bortezomib. Similar, siRNA knockdown of E6-AP and the E2 ligase Ubc9 increased cellular SOX9 amounts, supporting the notion that SOX9 may be ubiquitinated in hypertrophic chondrocytes by E6-AP and degraded by proteasomes. This is in accordance with the distribution of SOX9 levels, which are high in proliferating and prehypertrophic chondrocytes but low in hypertrophic chondrocytes, whereas E6-AP levels are high in hypertrophic chondrocytes and low in prehypertrophic chondrocytes. Furthermore, E6-AP-deficient mice showed SOX9 accumulation in chondrocytes and the brain. These findings support the concept that E6-AP regulates SOX9 levels in developing cartilage by acting as a ubiquitin ligase. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 49 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-12-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | SOX9 Transcription Factor Metabolism Ubiquitin-Protein Ligases Amino Acid Sequence Animals COS Cells Cell Line Cercopithecus Aethiops Chondrocytes HEK293 Cells Mice Mice, Knockout Molecular Sequence Data Protein Binding Proteomics RNA, Small Interfering Genetics Chemistry Ubiquitin-Conjugating Enzymes Antagonists & Inhibitors Deficiency Ubiquitination Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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