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).
DeSalle
L M
LM
Department of Pathology and Kaplan Comprehensive Cancer Center, MSB 548, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA.
Latres
E
E
Lin
D
D
Graner
E
E
Montagnoli
A
A
Baker
R T
RT
Pagano
M
M
Loda
M
M
D020816:Amino Acid Motifs; D000906:Antibodies / Q000276:immunology; D002453:Cell Cycle; D002460:Cell Line; D006801:Humans; D019169:Jurkat Cells; D015513:Oncogene Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D016160:Retinoblastoma Protein / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D043222:Ubiquitin Thiolesterase; D064570:Ubiquitin-Specific Proteases; D014452:Ubiquitins / Q000378:metabolism
D000906:Antibodies; D015513:Oncogene Proteins; D016160:Retinoblastoma Protein; C486203:USP4 protein, human; D014452:Ubiquitins; D043222:Ubiquitin Thiolesterase; D064570:Ubiquitin-Specific Proteases