| First Author | Gao X | Year | 2015 |
| Journal | FEBS J | Volume | 282 |
| Issue | 5 | Pages | 874-90 |
| PubMed ID | 25559396 | Mgi Jnum | J:237328 |
| Mgi Id | MGI:5811986 | Doi | 10.1111/febs.13186 |
| Citation | Gao X, et al. (2015) Poly(A)(+) mRNA-binding protein Tudor-SN regulates stress granules aggregation dynamics. FEBS J 282(5):874-90 |
| abstractText | 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. |
