RNA Recognition and Stress Granule Formation by TIA Proteins

被引：59

作者：

Waris, Saboora ^{[1
]}

Wilce, Matthew Charles James ^{[1
]}

Wilce, Jacqueline Anne ^{[1
]}

机构：

[1] Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2014年 / 15卷 / 12期

基金：

英国医学研究理事会; 澳大利亚研究理事会;

关键词：

RNA-binding proteins; mRNA; stress granule; translation; 5 '-oligopyrimidine terminal 5 '-oligopyrimidine (TOP) elements; RNA-recognition motif (RRM); T cell restricted intracellular antigen-1 (TIA-1); TIA-1 related protein (TIAR); prion-related domain (PRD); INTRACELLULAR ANTIGEN-1 TIA-1; AU-RICH ELEMENTS; MESSENGER-RNA; BINDING-PROPERTIES; STRANDED RNA; SITES; MOTIF; APOPTOSIS; SEQUENCE; PHOSPHORYLATION;

D O I：

10.3390/ijms151223377

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：

Stress granule (SG) formation is a primary mechanism through which gene expression is rapidly modulated when the eukaryotic cell undergoes cellular stresses (including heat, oxidative, viral infection, starvation). In particular, the sequestration of specifically targeted translationally stalled mRNAs into SGs limits the expression of a subset of genes, but allows the expression of heatshock proteins that have a protective effect in the cell. The importance of SGs is seen in several disease states in which SG function is disrupted. Fundamental to SG formation are the T cell restricted intracellular antigen (TIA) proteins (TIA-1 and TIA-1 related protein (TIAR)), that both directly bind to target RNA and self-associate to seed the formation of SGs. Here a summary is provided of the current understanding of the way in which TIA proteins target specific mRNA, and how TIA self-association is triggered under conditions of cellular stress.

引用

页码：23377 / 23388

页数：12

共 59 条

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