Journal
FEBS JOURNAL
Volume 282, Issue 5, Pages 874-890Publisher
WILEY
DOI: 10.1111/febs.13186
Keywords
PABP1; poly(A)(+) mRNA; processing bodies; stress granules; Tudor-SN
Categories
Funding
- National Science Foundation for Distinguished Young Scholars of China [31125012]
- NSFC [21305103, 31100967, 31170830, 31370749]
- China Postdoctoral Science Foundation [2013T60258]
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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.
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