Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions.
SGs are mRNA containing cytoplasmic structures that are assembled in response to stress. Tudor-SN protein is a ubiquitously expressed protein. Here, Tudor-SN protein was found to physiologically interact with G3BP, which is the marker and effector of SG. The kinetics of the assembly of SGs in the living cells demonstrated ... that Tudor-SN co-localizes with G3BP and is recruited to the same SGs in response to different stress stimuli. Knockdown of endogenous Tudor-SN did not inhibit the formation of SGs, but retarded the aggregation of small SGs into large SGs. Thus Tudor-SN may not be an initiator as essential as G3BP for the formation of SGs, but affects the aggregation of SGs. These findings identify Tudor-SN as a novel component of SGs.
Mesh Terms:
Animals, COS Cells, Carrier Proteins, Cercopithecus aethiops, Cytoplasmic Granules, Gene Knockdown Techniques, HeLa Cells, Humans, Nuclear Proteins, Protein Interaction Mapping, RNA, Small Interfering, Recombinant Fusion Proteins, Stress, Physiological
Animals, COS Cells, Carrier Proteins, Cercopithecus aethiops, Cytoplasmic Granules, Gene Knockdown Techniques, HeLa Cells, Humans, Nuclear Proteins, Protein Interaction Mapping, RNA, Small Interfering, Recombinant Fusion Proteins, Stress, Physiological
FEBS Lett.
Date: Aug. 20, 2010
PubMed ID: 20643132
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