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- Title
The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
- Authors
DeSalle, Lauren M; Latres, Esther; Lin, Douglas; Graner, Edgard; Montagnoli, Alessia; Baker, Rohan T; Pagano, Michele; Loda, Massimo
- Abstract
The ubiquitin pathway is involved in the proteolytic turnover of many short-lived cellular regulatory proteins. Since selective degradation of substrates of this system requires the covalent attachment of a polyubiquitin chain to the substrates, degradation could be counteracted by de-ubiquitinating enzymes (or isopeptidases) which selectively remove the polyubiquitin chain. Unp is a human isopeptidase with still poorly understood biological functions. Here, we show that cellular Unp specifically interacts with the retinoblastoma gene product (pRb). Oncogene (2001) 20, 5538–5542.
- Subjects
RETINOBLASTOMA; UBIQUITIN; CELL cycle; ONCOGENES
- Publication
Oncogene, 2001, Vol 20, Issue 39, p5538
- ISSN
0950-9232
- Publication type
Article
- DOI
10.1038/sj.onc.1204824