The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

被引：30

作者：

DeSalle, LM

Latres, E

Lin, D

Graner, E

Montagnoli, A

Baker, RT

Pagano, M ^{[1
]}

Loda, M

机构：

[1] Dana Farber Canc Inst, Dept Adult Oncol, Boston, MA 02115 USA

[2] NYU, Med Ctr, Dept Pathol, New York, NY 10016 USA

[3] NYU, Med Ctr, Caplan Comprehens Canc Ctr, New York, NY 10016 USA

[4] Harvard Univ, Brigham & Womens Hosp, Sch Med, Dept Pathol, Boston, MA 02115 USA

[5] Australian Natl Univ, John Curtin Sch Med Res, Canberra, ACT 2601, Australia

来源：

ONCOGENE | 2001年 / 20卷 / 39期

关键词：

Unp; retinoblastoma; isopeptidase; ubiquitin;

D O I：

10.1038/sj.onc.1204824

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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).

引用

页码：5538 / 5542

页数：5

共 30 条

[1]

Amerik AY, 1997, EMBO J, V16, P4826

[2] Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases [J].