Disease relevance of ILF3

• Conversely, NF90 activated the cytomegalovirus immediate-early promoter, to which it was not targeted [1].
• The results of size exclusion chromatography indicate that DRBP76 heterodimerizes with nuclear factor of activated T cells, 45 kDa (NF45), in neuronal but not in glioma cells [2].
• We isolated several ilf3 transcripts from a melanoma cDNA library and two corresponding genomic fragments, and report alternative splicing and polyadenylation site selection in the human ILF3 gene [3].
• The interaction of recombinant TCP80/NF90 with GCase mRNA was evaluated using the baculovirus/Sf9 insect cell system since these cells lack this protein [4].
• Here we describe a group of host factors designated as 'NFAR proteins' that are recruited by the replication machinery of bovine viral diarrhea virus, a close relative of the human pathogen hepatitis C virus [5].

Psychiatry related information on ILF3

• Because NFAR proteins are presumed components of the antiviral response, we suspect that viral recruitment may also serve to weaken cellular defense mechanisms [5].

High impact information on ILF3

• The nuclear export of NF90 is required for IL-2 mRNA stabilization [6].
• In nonstimulated cells, NF90 is mostly nuclear, but T cell activation results in its accumulation in the cytoplasm [6].
• NF90, a previously described RNA binding protein, binds to a subregion of the 3'UTR that contains several AREs and slows down the degradation of IL-2 mRNA [6].
• Further experimental data suggest that NFAR proteins mediate a circular conformation of the viral genome that may be important for the coordination of translation and replication [5].
• Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus [5].

Biological context of ILF3

• We find that the dsRBD of ILF3 functions as a novel nuclear export sequence (NES) in intact cells, and its ability to serve as an NES is dependent on the expression of the Kap [7].
• Using microinjection in the nucleus of HeLa cells and transfection experiments, we show here that formation of the cooperative RanGTP-dependent RNA/ILF3/exportin-5 complex promotes the co-transport of VA1 and ILF3 from the nucleus to the cytoplasm [8].
• ILF3 is a robust substrate for methylation by PRMT1 and can modulate PRMT1 activity in in vitro methylation assays [9].
• We used a GenBank sequence for the part of chromosome 19 corresponding to the ILF3 gene to determine the exon-intron organization of the entire gene which spans 38 kb and is divided into 21 exons [3].
• Cell cycle dependent intracellular distribution of two spliced isoforms of TCP/ILF3 proteins [10].

Anatomical context of ILF3

• The NF90 protein was found to be expressed not only in T-cells, but also in nonimmune HeLa cells [11].
• Mapping interleukin enhancer binding factor 3 gene (ILF3) to human chromosome 19 (19q11-qter and 19p11-p13.1) by polymerase chain reaction amplification of human-rodent somatic cell hybrid DNA templates [12].
• Time course analyses show that TCP80 functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes [13].
• Other VV mutants that produced excess dsRNA also inhibited protein binding to the IL-2 enhancer, suggesting that the presence of viral dsRNA has a role in retaining NF-90 in the cytosol and regulating IL-2 gene expression [14].
• Infection of Jurkat cells with a VV mutant that produces free dsRNA led to similar levels of induced NF-90 within the cell, but the protein remained localized within the cytosol [14].

Associations of ILF3 with chemical compounds

• CsA-sensitive purine-box transcriptional regulator in bronchial epithelial cells contains NF45, NF90, and Ku [15].
• This correlated with a 90% reduction in TCP80 phosphorylation in the presence of BIM [16].
• Four polyamide FilmTec membranes; three reverse osmosis/RO (BW-400, LE-440, XLE-440) and one nanofiltration/NF (NF-90); are being characterized according to pure water permeability (PWP), molecular weight cutoff (MWCO), hydrophobicity (contact angle), and surface charge (zeta potential) [17].
• ILF-3 was demonstrated to activate the synoviolin promoter via association with GABPalpha in rheumatoid synovial cells [18].

Physical interactions of ILF3

• JAZ also binds to ILF3, and surprisingly, this interaction is RNA independent, even though it requires the dsRNA binding domains of ILF3 [19].
• Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3 [8].
• Transfection assays showed that NF45 binds NF90 strongly and stimulates its ability to activate but not to inhibit gene expression [1].
• Nuclear factor 90 (NF90) was originally isolated in a complex that binds to the antigen recognition response element (ARRE-2) present in the interleukin-2 promoter [1].

Enzymatic interactions of ILF3

• NF90 is phosphorylated by PKR in its RNA-binding domain, and this reaction is partially blocked by the NF90 N-terminal region [20].

Regulatory relationships of ILF3

• Both NF110 isoforms are more active than NF90 isoforms in stimulating transcription from the proliferating cell nuclear antigen reporter in a transient expression system [21].
• Phosphorylation at Ser647 of NF90 up-regulated IL-2 production in response to CD28 costimulation [22].

Other interactions of ILF3

• Using an immunofluorescence analysis, we determined that ILF3 and PRMT1 co-localize in the nucleus [9].
• Formation of this complex is facilitated by the ability of both exportin-5 and ILF3 to mutually increase their apparent affinity for VA1 RNA [8].
• We have recently assigned the gene encoding the small NFAT subunit, NF45 (ILF3) to human chromosome 1 (1q11-qter and 1p11-p12) [12].
• This study indicates that the multiple cellular functions, i.e., translation control, interleukin-2 enhancer binding, or cell division, of TCP/ILF3 are fulfilled by alternatively spliced isoforms [10].
• It can also export the RNA binding proteins ILF3 and elongation factor EF1A [19].

Analytical, diagnostic and therapeutic context of ILF3

• Moreover, PRMT1 and ILF3 co-precipitate in immunoprecipitation assays and can be isolated together in "pull-down" experiments using recombinant fusion proteins [9].
• To resolve the genetic identity of NFAR-1 and -2, we carried out sequence analysis of genomic and cDNA NFAR clones and determined that the coding region of this gene spans 16.2 kb and comprises 21 exons [23].
• Cell fractionation studies showed that NF90 and its heteromeric partner, NF45, are predominantly nuclear and largely chromatin-associated [21].
• The DHS-22 binding protein(s) in THP-1 cells is (are) further confirmed by reactivity to an antibody against NF90, and we have demonstrated that the GST fusion protein of NF90 interacts with DHS-22 by electrophoretic gel mobility shift assay (EMSA) [24].
• These proteins were identified as the human proliferation associated protein, Ebp1, and human DRBP76 (double stranded RNA-binding protein 76) respectively, by MALDI (matrix-assisted laser-desorption ionization)-MS [25].

References