Disease relevance of RBM3

• However, cells depleted of mitochondria were still able to upregulate RBM3 and CIRP in response to hypoxia [1].

High impact information on RBM3

• NACA was recently defined as a coactivator of c-jun-mediated transcription factors in osteoblasts, and RBM3 as a protein from the heterogeneous nuclear ribonucleoprotein family [2].
• We report here the cloning of mouse Rbm3 cDNA, which encoded an 18-kd protein with 94% identity in amino acid sequence to that of human RBM3 [3].
• Host-encoded proteins hnRNP A2 and RBM3 may also interact with these viral factors to influence late gene expression [4].
• We also found an association of borderline significance (P=0.05) between the expression of RBM3, the large variant of RBM10 and wild-type p53 [5].
• Protein synthesis inhibitors cycloheximide and puromycin induced RBM3 transcripts, but cadmium chloride, H2O2, ethanol, and osmotic shock had no effect [6].

Biological context of RBM3

• Hypoxia-induced RBM3 or CIRP transcription was inhibited by the respiratory chain inhibitors NaN(3) and cyanide in a dose-dependent fashion [1].
• In NC65 cells, the kinetics of RBM3 induction was different from that of CIRP [6].
• Combined with the different tissue distribution of expression, these results suggest that RBM3 and CIRP play distinct roles in cold responses of human cells [6].

Anatomical context of RBM3

• RBM3 transcripts were constitutively expressed in all cell lines examined including K562, HepG2, NC65, HeLa, and T24 cells [6].

Other interactions of RBM3

• Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress [6].

References