A novel splice variant of supervillin, SV5, promotes carcinoma cell proliferation and cell migration

被引:14
作者
Chen, Xueran [1 ,2 ]
Yang, Haoran [2 ]
Zhang, Shangrong [1 ]
Wang, Zhen [1 ]
Ye, Fang [2 ]
Liang, Chaozhao [1 ]
Wang, Hongzhi [1 ,2 ]
Fang, Zhiyou [1 ,2 ]
机构
[1] Chinese Acad Sci, Hefei Inst Phys Sci, Ctr Med Phys & Technol, 350 Shushan Hu Rd, Hefei 230031, Anhui, Peoples R China
[2] Chinese Acad Sci, Canc Hosp, 350 Shushan Hu Rd, Hefei 230031, Anhui, Peoples R China
基金
中国国家自然科学基金;
关键词
Supervillin; Alternative splicing; Cell proliferation; Cell migration; MYOSIN-II ACTIVATION; F-ACTIN; ISOFORM; BINDING; PROTEIN; CANCER; CONTRACTILITY; CYTOSKELETON; CYTOKINESIS; ARCHVILLIN;
D O I
10.1016/j.bbrc.2016.11.013
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
Supervillin is an actin-associated protein that regulates actin dynamics by interacting with Myosin II, F-actin, and Cortactin to promote cell contractility and cell motility. Two splicing variants of human Supervillin (SV1 and SV4) have been reported in non-muscle cells; SV1 lacks 3 exons present in the larger isoform SV4. SV2, also called archvillin, is present in striated muscle; SV3, also called smooth muscle archvillin or SmAV, was cloned from smooth muscle. In the present study, we identify a novel splicing variant of Supervillin (SV5). SV5 contains a new splicing pattern. In the mouse tissues and cell lines examined, SV5 was predominantly expressed in skeletal and cardiac muscles and in proliferating cells, but was virtually undetectable in most normal tissues. Using RNAi and rescue experiments, we show here that SV5 displays altered functional properties in cancer cells, and regulates cell proliferation and cell migration. (C) 2016 Elsevier Inc. All rights reserved.
引用
收藏
页码:43 / 49
页数:7
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