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The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.

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).

Pubmed ID: 11571652


  • DeSalle LM
  • Latres E
  • Lin D
  • Graner E
  • Montagnoli A
  • Baker RT
  • Pagano M
  • Loda M



Publication Data

September 6, 2001

Associated Grants

  • Agency: NCI NIH HHS, Id: 5RO1-CA81755
  • Agency: NCI NIH HHS, Id: P30-CA16087
  • Agency: NCI NIH HHS, Id: R01-CA76584
  • Agency: NIGMS NIH HHS, Id: R01-GM57587
  • Agency: NCI NIH HHS, Id: R21-CA66229

Mesh Terms

  • Amino Acid Motifs
  • Antibodies
  • Cell Cycle
  • Cell Line
  • Humans
  • Jurkat Cells
  • Oncogene Proteins
  • Retinoblastoma Protein
  • Tumor Cells, Cultured
  • Ubiquitin Thiolesterase
  • Ubiquitins