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

FEBS Lett. 2010 Aug 20;584(16):3525-32. doi: 10.1016/j.febslet.2010.07.022. Epub 2010 Jul 17.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Chlorocebus aethiops
  • Cytoplasmic Granules / metabolism*
  • DNA Helicases
  • Endonucleases
  • Gene Knockdown Techniques
  • HeLa Cells
  • Humans
  • Nuclear Proteins / antagonists & inhibitors
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Poly-ADP-Ribose Binding Proteins
  • Protein Interaction Mapping
  • RNA Helicases
  • RNA Recognition Motif Proteins
  • RNA, Small Interfering / genetics
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Stress, Physiological

Substances

  • Carrier Proteins
  • Nuclear Proteins
  • Poly-ADP-Ribose Binding Proteins
  • RNA Recognition Motif Proteins
  • RNA, Small Interfering
  • Recombinant Fusion Proteins
  • Endonucleases
  • SND1 protein, human
  • DNA Helicases
  • G3BP1 protein, human
  • RNA Helicases