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Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Liakopoulos, Dimitris Buesgen, Thomas Brychzy, Alexander Jentsch, Stefan Pause, Arnim |
| Copyright Year | 1999 |
| Abstract | The von Hippel-Lindau tumor suppressor protein pVHL assembles with cullin-2 (hCUL-2) and elongin B/C forming a protein complex, CBCVHL, that resembles SKP1-CDC53-F-box protein ubiquitin ligases. Here, we show that hCUL-2 is modified by the conserved ubiquitin-like protein NEDD8 and that NEDD8-hCUL-2 conjugates are part of CBCVHL complexes in vivo. Remarkably, the formation of these conjugates is stimulated by the pVHL tumor suppressor. A tumorigenic pVHL variant, however, is essentially deficient in this activity. Thus, ligation of NEDD8 to hCUL-2 is linked to pVHL activity and may be important for pVHL tumor suppressor function. |
| File Format | PDF HTM / HTML |
| DOI | 10.1073/pnas.96.10.5510 |
| PubMed reference number | 10318914 |
| Journal | Medline |
| Volume Number | 96 |
| Issue Number | 10 |
| Alternate Webpage(s) | http://www.pnas.org/content/96/10/5510.full.pdf |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
