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

TitleThe de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
Publication TypeJournal Article
Year of Publication2001
AuthorsDeSalle LM, Latres E, Lin D, Graner E, Montagnoli A, Baker RT, Pagano M, Loda M
JournalOncogene
Volume20
Issue39
Pagination5538-42
Date Published2001 Sep 06
ISSN0950-9232
KeywordsAmino 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).

DOI10.1038/sj.onc.1204824
Alternate JournalOncogene
PubMed ID11571652
Grant List5RO1-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.

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