The role of cold‐inducible RNA binding protein in cell stress response

Abstract

Cold-inducible RNA binding protein (CIRP) was discovered after the cells were exposed to a moderate cold shock because its production was induced. Other cellular stresses such as ultraviolet light radiation and hypoxia also could increase its expression. Under stress conditions, CIRP could up regulate its own expression by self-transcriptional activation of alternative promoters. After relocating into cytoplasm from nucleus, CIRP assists cells in adapting to novel environmental conditions via stabilizing specific mRNAs and facilitating their translation. It not only participates in anti-apoptosis processes under mild hypothermia condition, but also protects cells from ultraviolet radiation and hypoxia induced senescence process. This article focuses on the possible mechanisms of its inducible expression, cytoprotective functions and carcinogenesis. In addition, extracellular CIRP has been shown to be a novel danger-associated molecular patter (DAMP) member and is able to induce inflammatory response. Finally, based on the distinct roles of CIRP in intracellular and extracellular conditions, a possible model of CIRP-mediated cell fate has been proposed.

Altered m6A modification of specific cellular transcripts affects Flaviviridae infection

“…We focused on two specific transcripts that gain or lose m 6 A during infection by all viruses 219 (DENV, ZIKV, WNV, and HCV) for further analysis: RIOK3 (gains) and CIRBP (loses). RIOK3 220 encodes a serine/threonine kinase and has been implicated in regulating antiviral signaling (Feng 221 et al, 2014;Takashima et al, 2015;Willemsen et al, 2017), while CIRBP encodes a stress-222 induced RNA-binding protein (Liao et al, 2017). Following viral infection, RIOK3 mRNA gains an 223 m 6 A peak in the 3' UTR close to the stop codon ( Figure 2A), and CIRBP mRNA shows reduced 224 m 6 A modification in the coding sequence of its last exon ( Figure 2B).…”

Hypothermia induces changes in the alternative splicing pattern of cold-inducible RNA-binding protein transcripts in a non-hibernator, the mouse

“…Cold-inducible RNA-binding protein (CIRBP) is one of the cold-shock proteins, for which expression is increased in response to cold stress (15,16,29). The protein has an RNA-recognition motif in the N-terminal region and an arginine-glycine-rich motif in the C-terminal region (10,11,31). CIRBP has the capacity to bind RNAs and thereby regulate the expression of various proteins at the post-transcriptional level through modulating mRNA splicing, stability and transport (10,11,14,25,28,(30)(31)(32).…”

Proteomics provides insights into the inhibition of Chinese hamster V79 cell proliferation in the deep underground environment

“…In the present study, proteins involved in oxidation-reduction reactions, including oxygen binding, oxygen transporter activity, and hemoglobin subunits (G3ICM8, hemoglobin subunit epsilon-Y2; G3ICM5, hemoglobin subunit beta; G3HBR8, hemoglobin subunit alpha) were up-regulated in V79 cells cultured in the DUGL. Hemoglobin is a major host respiratory protein that can also be specifically activated by pathogens to produce ROS [28]. The hemoglobin subunit epsilon 1 (HBE1) has been implicated in the radiation sensitivity and resistance of colorectal cancer cells [29] , and hemoglobin over expression affected O 2 homeostasis or suppressed oxidative stress in murine MN9D and SV40-MES13 cells, respectively.…”