title: The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
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).
authors.affiliation: Department of Pathology and Kaplan Comprehensive Cancer Center, MSB 548, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA.
authors.forename: L M
authors.initials: LM
authors.lastname: DeSalle
authors.forename: E
authors.initials: E
authors.lastname: Latres
authors.forename: D
authors.initials: D
authors.lastname: Lin
authors.forename: E
authors.initials: E
authors.lastname: Graner
authors.forename: A
authors.initials: A
authors.lastname: Montagnoli
authors.forename: R T
authors.initials: RT
authors.lastname: Baker
authors.forename: M
authors.initials: M
authors.lastname: Pagano
authors.forename: M
authors.initials: M
authors.lastname: Loda
mesh_terms: 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
chemical_list: D000906:Antibodies; D015513:Oncogene Proteins; D016160:Retinoblastoma Protein; C486203:USP4 protein, human; D014452:Ubiquitins; D043222:Ubiquitin Thiolesterase; D064570:Ubiquitin-Specific Proteases