Poly(A)+ mRNA‐binding protein Tudor‐SN regulates stress granules aggregation dynamics. (26th January 2015)

• Record Type: Journal Article
• Authors: Gao, Xingjie; Fu, Xue; Song, Juan; Zhang, Yi; Cui, Xiaoteng; Su, Chao; Ge, Lin; Shao, Jie; Xin, Lingbiao; Saarikettu, Juha; Mei, Mei; Yang, Xi; Wei, Minxin; Silvennoinen, Olli; Yao, Zhi; He, Jinyan; Yang, Jie
• Is Part Of: FEBS journal. Volume 282:Number 5(2015)
• Page Start: 874
• Page End: 890
• Publication Date: 2015-01-26
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.13186
• Languages: English
• ISSNs: 1742-464X

Abstract

<abstract abstract-type="main" id="febs13186-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Stress granules (SGs) and processing bodies (PBs) comprise the main types of cytoplasmic RNA foci during stress. Our previous data indicate that knockdown of human Tudor staphylococcal nuclease (Tudor‐SN) affects the aggregation of SGs. However, the precise molecular mechanism has not been determined fully. In the present study, we demonstrate that Tudor‐SN binds and colocalizes with many core components of SGs, such as poly(A)⁺ mRNA binding protein 1, T‐cell internal antigen‐1‐related protein and poly(A)⁺ mRNA, and SG/PB sharing proteins Argonaute 1/2, but not PB core proteins, such as decapping enzyme 1 a/b, confirming that Tudor‐SN is an SG‐specific protein. We also demonstrate that the Tudor‐SN granule actively communicates with the nuclear and cytosolic pool under stress conditions. Tudor‐SN can regulate the aggregation dynamics of poly(A)⁺ mRNA‐containing SGs and selectively stabilize the SG‐associated mRNA during cellular stress.</p> </abstract>