Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions

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• 作者：Xingjie Gao ; Lin Ge ; Jie Shao ; Chao Su ; Hong Zhao ; Juha Saarikettu ; Xuyang Yao ; Zhi Yao ; Olli Silvennoinen ; Jie Yang
• 关键词：Tudor-SN ; G3BP ; Stress granule ; Tudor domain containing protein
• 刊名：FEBS Letters
• 出版年：2010
• 出版时间：20 August 2010
• 年：2010
• 卷：584
• 期：16
• 页码：3525-3532
• 全文大小：1756 K

文摘

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)