A novel p53-binding domain in CUL7

被引：26

作者：

Kasper, Jocelyn S.

Arai, Takehiro

DeCaprio, James A.

机构：

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

[2] Brigham & Womens Hosp, Dept Med, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Boston, MA USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 348卷 / 01期

关键词：

cullin RING ligase; SKP-cullin-F box; CUL7; p53; PARC; ubiquitin-protein ligases; sequence homology; tumor suppressors;

D O I：

10.1016/j.bbrc.2006.07.013

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：

CUL7 is a member of the cullin RING ligase family and forms an SCF-like complex with SKP1 and FBXW8. CUL7 is required for normal mouse embryonic development and cellular proliferation, and is highly homologous to PARC, a p53-associated, parkin-like cytoplasmic protein. We determined that CUL7, in a manner similar to PARC, can bind directly to p53. but does not affect p53 expression. We identified a discrete, co-linear domain in CUL7 that is conserved in PARC and HERC2, and is necessary and sufficient for p53-binding. The presence of p53 stabilized expression of this domain and we demonstrate that this p53-binding domain of CUL7 contributes to the cytoplasmic localization of CULT The results support the model that p53 plays a role in regulation of CUL7 activity, (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：132 / 138

页数：7

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