
doi: 10.1111/febs.13186
pmid: 25559396
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.
Cell Nucleus, DNA Helicases, Nuclear Proteins, Cytoplasmic Granules, Endonucleases, Poly(A)-Binding Protein I, Insulin-Like Growth Factor Binding Protein 2, Oxidative Stress, Cytosol, Polyribosomes, Argonaute Proteins, Endoribonucleases, Humans, Protein Interaction Maps, Eukaryotic Initiation Factors, Carrier Proteins, Poly A, Poly-ADP-Ribose Binding Proteins, RNA Helicases, HeLa Cells
Cell Nucleus, DNA Helicases, Nuclear Proteins, Cytoplasmic Granules, Endonucleases, Poly(A)-Binding Protein I, Insulin-Like Growth Factor Binding Protein 2, Oxidative Stress, Cytosol, Polyribosomes, Argonaute Proteins, Endoribonucleases, Humans, Protein Interaction Maps, Eukaryotic Initiation Factors, Carrier Proteins, Poly A, Poly-ADP-Ribose Binding Proteins, RNA Helicases, HeLa Cells
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