4.5 Article

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

Journal

FEBS LETTERS
Volume 584, Issue 16, Pages 3525-3532

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.07.022

Keywords

Tudor-SN; G3BP; Stress granule; Tudor domain containing protein

Funding

  1. Ministry of Science and Technology of China [2007AA02Z115]
  2. NSFC [90919032, 30970562, 30670441]
  3. 973 program [2009CB918903]
  4. Specialized Fund for the Doctoral Program of Higher Education [20091202110001]
  5. TSTC [08ZCGHHZ01900, 08JCYBJC07700]
  6. Tianjin Educational Committee Foundation [2008ZD01]
  7. Medical Research Council of Academy of Finland
  8. Finnish Foundation for Cancer Research

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available