Cold-induced RNA-binding protein (CIRBP) is a 172-residue, multifunctional sensor protein that was first isolated as a protein induced in mouse fibroblasts cultured at 32ºC. Conversely, CIRBP expression decreases in cells or tissues subjected to increased temperature. The CIRBP protein is composed of an amino-terminal RNA-binding domain and a carboxyl-terminal, glycine-rich domain. Stressful stimuli, such as hypoxia, heat shock, osmotic shock, or oxidative conditions, lead to translocation of CIRBP from the nucleus to cytoplasmic stress granules through a mechanism involving CIRBP methylation-dependent nuclear export. CIRBP plays a role in regulating apoptosis and preserving the stemness of neural stem cells at moderately low temperatures. Research studies demonstrate that CIRBP contributes to the regulation of circadian rhythm through post-translational modulation of CLOCK expression.
