From skeletal muscle to cancer: Insights learned elucidating the function of tropomyosin

被引：25

作者：

Choi, Cheolwon ^{[1
]}

Kim, Dayoung ^{[1
]}

Kim, Sabina ^{[2
]}

Jeong, SukYeong ^{[1
]}

Song, Eunsol ^{[1
]}

Helfman, David M. ^{[1
,2
]}

机构：

[1] Korea Adv Inst Sci & Technol, Dept Biol Sci, Taejon 305701, South Korea

[2] Korea Adv Inst Sci & Technol, Grad Sch Nanosci & Technol WCU, Taejon 305701, South Korea

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2012年 / 177卷 / 01期

基金：

新加坡国家研究基金会;

关键词：

Tropomyosin; Cytoskeleton; Cell motility; Cancer; Coiled-coil; MOLECULAR-WEIGHT TROPOMYOSINS; RAS-TRANSFORMED FIBROBLASTS; CHICKEN-EMBRYO FIBROBLASTS; SIGNAL-REGULATED KINASE; TUMOR-SUPPRESSOR; NONMUSCLE TROPOMYOSIN; ACTIN CYTOSKELETON; TGF-BETA; ISOFORM EXPRESSION; OXIDATIVE STRESS;

D O I：

10.1016/j.jsb.2011.11.016

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 tropomyosins (Tms) are a family of actin filament binding proteins that possess a simple dimeric alpha-helical coiled-coil structure along their entire length. Our knowledge of Tm structure and function has greatly expanded since they were first discovered in skeletal muscle almost 65 years ago. In multicellular organisms they exhibit extensive cell type specific isoform diversity. In this essay we discuss the genetic mechanisms by which this diversity is generated and its significance to actin-based cellular functions. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：63 / 69

页数：7

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