Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel–Lindau tumor suppressor function
AUTOR(ES)
Liakopoulos, Dimitris
FONTE
The National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=21890Documentos Relacionados
- The von Hippel–Lindau tumor suppressor protein is a component of an E3 ubiquitin–protein ligase activity
- Transcription-Dependent Nuclear-Cytoplasmic Trafficking Is Required for the Function of the von Hippel-Lindau Tumor Suppressor Protein
- Identification of the von Hippel–Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
- Von Hippel-Lindau disease.
- Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products