PRL-3 activates NF-κB signaling pathway by interacting with RAP1

被引：26

作者：

Lian, Shenyi ^{[1
]}

Meng, Lin ^{[1
]}

Liu, Caiyun ^{[1
]}

Xing, Xiaofang ^{[1
]}

Song, Qian ^{[1
]}

Dong, Bin ^{[2
]}

Han, Yong ^{[1
]}

Yang, Yongyong ^{[1
]}

Peng, Lirong ^{[3
]}

Qu, Like ^{[1
]}

Shou, Chengchao ^{[1
]}

机构：

[1] Peking Univ, Canc Hosp & Inst, Dept Biochem & Mol Biol, Key Lab Carcinogenesis & Translat Res,Minist Educ, Beijing 100142, Peoples R China

[2] Peking Univ, Canc Hosp & Inst, Dept Pathol, Key Lab Carcinogenesis & Translat Res,Minist Educ, Beijing 100142, Peoples R China

[3] Univ S Florida, Coll Med, H Lee Moffitt Canc Ctr & Res Inst, Dept Mol Oncol, Tampa, FL 33612 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2013年 / 430卷 / 01期

基金：

中国国家自然科学基金;

关键词：

PRL-3; RAP1; NF-kappa B; Cancer; GENE-EXPRESSION; TYROSINE PHOSPHATASES; COLORECTAL-CANCER; PROTEIN COMPLEX; METASTASIS; INVASION; OVEREXPRESSION; INFLAMMATION; INHIBITION; MIGRATION;

D O I：

10.1016/j.bbrc.2012.11.036

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：

Phosphatase of regenerating liver (PRL-3) promotes cancer metastasis through enhanced cell motility and invasiveness, however its role in tumorigenesis remains unclear. Herein, we reported that PRL-3 interacts with telomere-related protein RAP1. PRL-3 promotes the cytosolic localization of RAP1, which is counteracted by silencing of PRL-3. Immunohistochemical staining of colon cancer tissue array (n = 170) revealed that high level of PRL-3 associates with cytosolic localization of RAP1 (p = 0.01). Microarray analysis showed that PRL-3 regulates expression of diverse genes and enhances phosphorylation of p65 subunit of NF-kappa B in a RAP1-dependent manner. Furthermore, PRL-3 transcriptionally activates RAP1 expression, which is counteracted by ablating p65. Therefore, our results demonstrate PRL-3 as a novel regulator of NF-kappa B signaling pathway through RAP1. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：196 / 201

页数：6

共 30 条

[1] A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends [J].