Rbfox RNA-binding proteins play important roles in the regulation of alternative 
pre-mRNA splicing, but their role in other gene regulatory mechanisms is not 
well understood. Here, we show that Rbfox2 is a novel constituent of cytoplasmic 
stress granules, the translational silencing machinery assembled in response to 
cellular stress. We also show that the RNA binding activity of the Rbfox family 
protein is crucial for its localization into stress granules. To investigate the 
role of Rbfox2 in stress granules we used RNA-immunoprecipitation sequencing to 
identify cytoplasmic transcriptome-wide targets of Rbfox2. We report that a 
subset of cell cycle-related genes including retinoblastoma 1 is the target of 
Rbfox2 in cytoplasmic stress granules, and Rbfox2 regulates the retinoblastoma 1 
mRNA and protein expression levels during and following stress exposure. Our 
study proposes a novel function for Rbfox2 in cytoplasmic stress granules.