CDK11p58 represses vitamin D receptor-mediated transcriptional activation through promoting its ubiquitin-proteasome degradation

被引：20

作者：

Chi, Yayun

Hong, Yi

Zong, Hongliang

Wang, Yanlin

Zou, Weiying

Yang, Junwu

Kong, Xiangfei

Yun, Xiaojing

Gu, Jianxin ^{[1
]}

机构：

[1] Fudan Univ, Shanghai Med Coll, Ctr Gene Res, Shanghai 200032, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 386卷 / 03期

基金：

中国国家自然科学基金;

关键词：

CDK11(p58); Vitamin D receptor; Transcription; Ubiquitination; OSTEOBLASTIC CELLS; PROTEIN; PATHWAY; PROLIFERATION; COMPLEX; ELEMENT; BINDING; SYSTEM; SITE; VDR;

D O I：

10.1016/j.bbrc.2009.06.061

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：

Vitamin D receptor (VDR) is a member of the nuclear receptor superfamily and regulates transcription of target genes. In this study, we identified CDK11(p58) as a novel protein involved ill the regulation of VDR. CDK11(p58), a member of the large family of p34cdc2-related kinases, is associated with cell cycle progression, tumorigenesis, and apoptotic signaling. Our study demonstrated that CDK11(p58) interacted with VDR and repressed VDR-dependent transcriptional activation. Furthermore, overexpression of CDK11(p58), decreased the stability of VDR through promoting its ubiquitin-proteasome-mediated degradation. Taken together, these results suggest that CDK11(p58) is involved in the negative regulation of VDR. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：493 / 498

页数：6

共 30 条

[1] AP-1 and vitamin D receptor (VDR) signaling pathways converge at the rat osteocalcin VDR element:: Requirement for the internal activating protein-1 site for vitamin D-mediated trans-activation [J].