Abstract
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. Structured summary MINT- 7968768, MINT- 7968779: Tudor-SN (uniprotkb: Q7KZF4) physically interacts (MI: 0915) with G3BP (uniprotkb: Q13283) by anti bait coimmunoprecipitation (MI: 0006) MINT- 7968800: Tudor-SN (uniprotkb: Q7KZF4) and TIA-1 (uniprotkb: P31483) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT- 7968789: Tudor-SN (uniprotkb: Q7KZF4) and G3BP (uniprotkb: Q13283) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416)
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