The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein. Academic Article uri icon

Overview

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).

publication date

  • September 6, 2001

Research

keywords

  • Oncogene Proteins
  • Retinoblastoma Protein

Identity

Scopus Document Identifier

  • 0035817801

Digital Object Identifier (DOI)

  • 10.1038/sj.onc.1204824

PubMed ID

  • 11571652

Additional Document Info

volume

  • 20

issue

  • 39