Journal
FEBS LETTERS
Volume 584, Issue 16, Pages 3525-3532Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.07.022
Keywords
Tudor-SN; G3BP; Stress granule; Tudor domain containing protein
Funding
- Ministry of Science and Technology of China [2007AA02Z115]
- NSFC [90919032, 30970562, 30670441]
- 973 program [2009CB918903]
- Specialized Fund for the Doctoral Program of Higher Education [20091202110001]
- TSTC [08ZCGHHZ01900, 08JCYBJC07700]
- Tianjin Educational Committee Foundation [2008ZD01]
- Medical Research Council of Academy of Finland
- Finnish Foundation for Cancer Research
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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.
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