Disease relevance of TRIM27

• Furthermore, ablation of RFP in U2OS osteosarcoma cells augments a transcriptional program indicative of lineage-specific differentiation in response to Rb [1].
• Using AH7974 (rat ascites hepatoma) and Raji (human Burkitt lymphoma) cells, we demonstrated strong association of RFP with the nuclear matrix [2].
• To further characterize the RFP protein, we developed a polyclonal antibody against the product synthesized from a fragment of the RFP cDNA expressed in Escherichia coli [2].
• RFP immunoreactivity was seen uniformly and specifically in 12 of the 13 pure seminomas examined [3].
• The catalytic activities of Ret tyrosine kinases as the products of oncogene RET with multiple endocrine neoplasia type 2A (Ret-MEN2A) or 2B (Ret-MEN2B) mutations and the hybrid gene from c-RET and RFP (Rfp-Ret) were higher than those of c-Ret [4].

Psychiatry related information on TRIM27

• Extending the RFP to a matrix evaluation form allows input from all persons involved in the decision-making process and displays the information in a clear manner, making the overall decision much easier [5].

High impact information on TRIM27

• RFP binds to Rb and prevents the degradation of the EID-1 inhibitor of histone acetylation and differentiation [1].
• We present evidence here that the RET finger protein (RFP)/tripartite motif protein 27 (TRIM 27) inhibits gene transcription activation by Rb but does not affect gene repression [1].
• Selective ablation of retinoblastoma protein function by the RET finger protein [1].
• To probe the consequences of such endogenous neurotrophin distribution, we produced 'donor neurons' in ferret cortex brain slices that co-expressed brain-derived neurotrophic factor (BDNF) and red fluorescent protein (RFP) [6].
• We generated heterokaryons that contained GFP- and RFP-tagged caveolae by fusing cells expressing Cav1-GFP and -RFP, respectively, and showed that even when activated, individual caveolar domains underwent little exchange of Cav1 [7].

Chemical compound and disease context of TRIM27

• METHODS: Human prostate cancer PC-3 cells were transduced with the pLNCX2-DsRed-2-RFP retroviral vector containing the RFP and neomycin-resistance genes [8].

Biological context of TRIM27

• Here we show that RFP interacts with Enhancer of Polycomb (EPC) and strongly represses the gene transcription [9].
• Using the luciferase reporter-gene assay, we found that they repress the gene transcription activity independent of the differences of enhancers and promoters used, although the repressive activity of RFP was much stronger than that of EPC [9].
• These results suggested that RFP may be involved in the epigenetic gene silencing mechanism cooperating with Polycomb group proteins and that EPC is a unique molecule with both repressive and transactivating activities [9].
• These results demonstrate that the intracellular location and the transcriptional activity of RFP are modified by PIAS proteins which possess SUMO E3 ligase activities and suggest that they may play a co-operative role in spermatogenesis [10].
• Moreover, in situ hybridization shows that RFP, butyrophilin, and MOG map to the human chromosome 6p21.3-6p22 region and are thus close to the MHC class I genes [11].

Anatomical context of TRIM27

• Although RFP is reported to be a nuclear protein that is present in the nuclear matrix, its function is largely unknown [9].
• Furthermore, the functional importance of the association of Mi-2 beta and RFP was confirmed by using Rfp-/- fibroblasts [12].
• Ret finger protein (RFP) is a nuclear protein that is highly expressed in testis and in various tumor cell lines [10].
• Finally, regulatory protein T-lymphocyte 1 (Rpt-1) shares similarities with the N-terminal halves of RFP, 52-kD SS-A/Ro, and XNF7, but not with the B30-2-like domain [11].
• Western blot analysis showed that RFP was identified as a 58 kDa protein in cell lysates from four human and rodent cell lines and from mouse testis [2].

Associations of TRIM27 with chemical compounds

• RET finger protein (RFP) belongs to the large B-box RING finger protein family and is known to become oncogenic by fusion with RET tyrosine kinase [9].
• When treated with retinoic acid, rfp reassociates with the NBs in a pattern similar to non APL cells [13].
• Transcriptional repression by RFP was trichostatin A sensitive and did not involve an Id-like mechanism or ubiquitination with subsequent degradation of bHLH proteins [14].
• However, when the host mice were pretreated with cyclophosphamide, the HCT-116-GFP-RFP cells also survived and formed colonies in the liver after portal vein injection [15].
• Mutation of this NES or treatment with leptomycin B abrogated the nuclear export of RFP in NIH3T3 cells [16].

Co-localisations of TRIM27

• Additionally, we found that rfp colocalizes with PML-RARA protein produced in APL patients [13].

Regulatory relationships of TRIM27

• To obtain the dual-color cells, red fluorescent protein (RFP) was expressed in the cytoplasm of HT-1080 human fibrosarcoma cells, and green fluorescent protein (GFP) linked to histone H2B was expressed in the nucleus [17].
• The RFP-expressing hMSCs were enriched by high-speed flow cytometry and maintained their potential to differentiate along adipogenic or osteogenic lineages [18].

Other interactions of TRIM27

• Microspherule protein 1, Mi-2beta, and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription [19].
• These results suggest that rfp, along with the other known/unknown components of PML NBs, have an important role in regulating cellular growth and differentiation [13].
• RFP functions as a transcriptional repressor and associates with Enhancer of Polycomb 1 (EPC1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex [10].
• Co-localization and association of Mi-2, RFP, and histone deacetylase 1 suggested that these proteins cooperate in transcriptional repression [12].
• Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities [12].

Analytical, diagnostic and therapeutic context of TRIM27

• We also found that MCRS1, Mi-2beta, and RFP were associated with rDNA using a chromatin immunoprecipitation assay [19].
• Yeast two-hybrid assays revealed that MCRS1 bound to the ATPase/helicase region of Mi-2beta and the coiled-coil region of RFP [19].
• We characterized the complex of IL-6-RFP and fluorescently labeled IL-6 (YFPIL-6) by blue native PAGE and gel filtration [20].
• In this study, we examined the expression of RFP and EPC1 in mouse tissues by immunoblotting as well as their interaction by a pull-down assay [21].
• This study examined the RFP expression in normal and tumor tissues by immunohistochemistry [22].

References