Evidence that cell surface localization of serine protease activity facilitates cleavage of the protease activated receptor CDCP1

被引：5

作者：

He, Yaowu ^{[1
]}

Reid, Janet C. ^{[1
]}

He, Hui ^{[1
]}

Harrington, Brittney S. ^{[1
]}

Finlayson, Brittney ^{[1
]}

Khan, Tashbib ^{[1
]}

Hooper, John D. ^{[1
]}

机构：

[1] Univ Queensland, Mater Res Inst, Translat Res Inst, 37 Kent St, Woolloongabba, Qld 4102, Australia

来源：

BIOLOGICAL CHEMISTRY | 2018年 / 399卷 / 09期

基金：

澳大利亚国家健康与医学研究理事会; 澳大利亚研究理事会;

关键词：

cancer; CDCP1; CUB domain containing protein 1; serine protease; DOMAIN-CONTAINING PROTEIN-1; CUB-DOMAIN; TYROSINE PHOSPHORYLATION; ELEVATED CDCP1; BREAST-CANCER; PKC-DELTA; CARCINOMA; SURVIVAL; IDENTIFICATION; SUBSTRATE;

D O I：

10.1515/hsz-2017-0308

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 cellular receptor CUB domain containing protein 1 (CDCP1) is commonly elevated and functionally important in a range of cancers. CDCP1 is cleaved by serine proteases at adjacent sites, arginine 368 (R368) and lysine 369 (K369), which induces cell migration in vitro and metastasis in vivo. We demonstrate that membrane localization of serine protease activity increases efficacy of cleavage of CDCP1, and that both secreted and membrane anchored serine proteases can have distinct preferences for cleaving at CDCP1-R368 and CDCP1-K369. Approaches that disrupt membrane localization of CDCP1 cleaving serine proteases may interfere with the cancer promoting effects of CDCP1 proteolysis.

引用

页码：1091 / 1097

页数：7

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