Disease relevance of SFRS11

• This functional conservation, together with the common replication strategies of positive-stranded RNA viruses, suggests that RCK/p54 may also play a role in the replication of positive-stranded RNA viruses that infect humans [1].
• Xenopus Xp54 and Human RCK/p54 Helicases Functionally Replace Yeast Dhh1p in Brome Mosaic Virus RNA Replication [1].
• Human rck/p54, a product of the gene cloned at the breakpoint of t(11; 14) (q23;q32) chromosomal translocation on 11q23 in B-cell lymphoma, is a member of the DEAD-box RNA helicase family [2].
• The cDNA for a 54-kDa nuclear protein (p54) has been cloned from a human hepatoma expression library [3].
• Overexpression of a DEAD box/RNA helicase protein, rck/p54, in human hepatocytes from patients with hepatitis C virus-related chronic hepatitis and its implication in hepatocellular carcinogenesis [4].

High impact information on SFRS11

• Here, we show that hCcr4, hDcp1b, hLsm, and rck/p54 proteins related to 5'-3' mRNA decay also localize to these structures, whereas DcpS, which is involved in cap nucleotide catabolism, is nuclear [5].
• Indirect immunofluorescence studies in HeLa cells show that p54 is distributed throughout the nucleus in a speckled pattern, with an additional diffuse labeling of the nucleus excluding the nucleoli [3].
• Contained within p54 is an arginine/serine-rich region similar to segments of several proteins that participate in pre-mRNA splicing including the 70-kDa component of U1 small nuclear and "suppressor-of-white-apricot" proteins [3].
• Sedimentation analysis of HeLa cell extracts on sucrose gradients showed that p54 migrates at 4-6 S, indicating that the protein is not a tightly associated component of snRNPs [3].
• SRp54 (SFRS11), a regulator for tau exon 10 alternative splicing identified by an expression cloning strategy [6].

Chemical compound and disease context of SFRS11

• The expression of p54 was colocalized with the terminal deoxynucleotidyl transferase-mediated biotinylated UTP nick end labeling-positive nuclei in glutamate-treated cerebellar granule neurons (CGNs) and in ischemic neurons located in the infarct core after focal cerebral ischemia, suggesting that p54 might be involved in neuronal death [7].

Biological context of SFRS11

• Functional properties of p54, a novel SR protein active in constitutive and alternative splicing [8].
• Here, we demonstrate a direct interaction between topoisomerase I and pyrimidine tract binding protein-associated splicing factor (PSF), a cofactor of RNA splicing, which forms heterodimers with its smaller homolog, the nuclear RNA-binding protein of 54 kDa (p54) [9].
• Over-expression of rck/p54 in HeLa cells caused growth inhibition and cell cycle arrest at G2/M with down-regulation of c-myc expression [2].
• Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54 [10].
• The kinetics of p54 induction were first order over a period of about 2-8 h after a lag of about 1 h [11].

Anatomical context of SFRS11

• Consistent with its identification as an SR protein, p54 can function as a constitutive splicing factor in complementing splicing-deficient HeLa cell S100 extract [8].
• These results suggest that polypeptide p54 may play an important role in the antiviral action of rIFN-gamma in human amnion U cells [11].
• Growth inhibition by overexpression of human DEAD box protein rck/p54 in cells of a guinea pig cell line [12].
• By this approach, two new proteins induced in differentiating cells, p57 and p54, were identified in cytoskeletal preparations enriched in intermediate filaments [13].
• Chloroplast RNA-binding protein p54 is an endoribonuclease required for 3'end-processing of plastid precursor transcripts [14].

Associations of SFRS11 with chemical compounds

• Crystals of Nc-rck/p54 were grown to a size suitable for X-ray structure analysis using polyethylene glycol 3350 as the precipitant [15].
• Kinase treatment of p54 prior to oxidation by glutathione resulted in highest levels of activation, suggesting that phosphorylation and redox state act together to control p54 activity in vitro and possibly also in vivo [14].
• Soon after rehydration in seed germination, p54 mRNA disappears and is no longer detectable in vegetative tissues, except in response to hydric stress (exposure to abscisic acid, osmolites or desiccation). p16 can be recovered from nuclei cross-linked to histone H3, when the disulfide bridges that occur in vivo are preserved [16].

Regulatory relationships of SFRS11

• The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction [9].

Analytical, diagnostic and therapeutic context of SFRS11

• The overexpression of rck/p54 was confirmed by Western blot and RT-PCR analysis [12].
• We examined the expression of rck/p54 in 29 cases of HCV-related chronic hepatitis and eight cases of hepatocellular carcinoma by immunohistochemistry and Western blot analysis [4].
• Crystallization and X-ray analysis of the N-terminal core domain of a tumour-associated human DEAD-box RNA helicase, rck/p54 [15].
• As measured by immunoprecipitation of [35S]methionine pulse-labeled extracts or by immunoblot analysis of unlabeled extracts, the synthesis of p54 was greatly elevated in three human cell lines treated with IFN-gamma, amnion U, fibroblast GM2767, and fibroblast F153 [17].
• EBV-specific antibodies were measured with novel ELISAs, utilizing the recombinant antigens p72 (for anti-EBV nuclear antigen [EBNA]1-IgG), p54, and p138 (anti-early antigen [EA]-IgM, -IgG, -IgA) in a follow-up study of 79 renal transplant recipients [18].

References