Title | The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein. |
Publication Type | Journal Article |
Year of Publication | 2001 |
Authors | DeSalle LM, Latres E, Lin D, Graner E, Montagnoli A, Baker RT, Pagano M, Loda M |
Journal | Oncogene |
Volume | 20 |
Issue | 39 |
Pagination | 5538-42 |
Date Published | 2001 Sep 06 |
ISSN | 0950-9232 |
Keywords | Amino Acid Motifs, Antibodies, Cell Cycle, Cell Line, Humans, Jurkat Cells, Oncogene Proteins, Retinoblastoma Protein, Tumor Cells, Cultured, Ubiquitin Thiolesterase, Ubiquitin-Specific Proteases, Ubiquitins |
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). |
DOI | 10.1038/sj.onc.1204824 |
Alternate Journal | Oncogene |
PubMed ID | 11571652 |
Grant List | 5RO1-CA81755 / CA / NCI NIH HHS / United States P30-CA16087 / CA / NCI NIH HHS / United States R01-CA76584 / CA / NCI NIH HHS / United States R01-GM57587 / GM / NIGMS NIH HHS / United States R21-CA66229 / CA / NCI NIH HHS / United States |
Related Faculty:
Massimo Loda, M.D.