Journal
ONCOGENE
Volume 20, Issue 39, Pages 5538-5542Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.onc.1204824
Keywords
Unp; retinoblastoma; isopeptidase; ubiquitin
Funding
- NCI NIH HHS [P30-CA16087, R01-CA76584, R21-CA66229, 5RO1-CA81755] Funding Source: Medline
- NIGMS NIH HHS [R01-GM57587] Funding Source: Medline
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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).
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