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
收藏
页码：132 / 138
页数：7
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