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The double stranded RNA (dsRNA)-dependent, Ser/Thr protein kinase, PKR, is encoded by an IFN-inducible gene and is critical for the anti-viral responses mediated by IFN. Interaction with activators such as heparin, dsRNA, and the dsRNA-binding proteins (DRBPs), DRBP76, PACT, and RAX, induces PKR autophosphorylation and activation. DRBP76 was identified through its binding to dsRNA and PKR. In addition, DRBP76 has been identified as the alternatively spliced nuclear phosphoproteins of 90kDa (NFAR-1/NF90) and 110kDa (NFAR-2), as well as M-phase phosphoprotein (MPP4), translational control protein 80 (TCP80), and interleukin enhancer binding factor 3 (ILF3). DRBP76 contains a bi-partite nuclear localization signal at amino acids 369-373 and 386-394, two DRB domains in the C-terminal half, and a C-terminal RG2 domain that is present in many RNA binding proteins. DRBP76 binds pre-mRNAs and spliced mRNAs, co-localizes with PKR in the nucleus, and is phosphorylated by PKR and possibly cyclin-dependent kinases. Thus, DRBP76 may be one of multiple DRBP variants, which associate with PKR and regulate RNA translation.Immunofluorescence, Western Blotting
