Disease relevance of TCEB3

• The survival curve for patients with SIII metastases approaches that of patients in the pre-SLNE era who underwent delayed lymph node dissection for subsequently detected nodal macrometastases [1].
• Labeling of Ehrlich ascites cells with radioactive uridine and a subsequent chase in the presence of RNA-synthesis inhibitors shows that radioactivity was incorporated first in precursor particles with a density of 1.48 g/cm3 and then subsequently appeared in SIII and SII particles [2].

High impact information on TCEB3

• Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein [3].
• Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II [3].
• The von Hippel-Lindau (VHL) tumour suppressorgene product is believed to be involved in the down-regulation of transcriptional elongation by preventing the association of elongin B and C with the catalytic subunit elongin A [4].
• At least two gDMRs mapped near imprinted genes, HYMA1 and a novel homolog of Elongin A and Elongin A2, which we term Elongin A3 [5].
• The heterodimeric Elongin BC complex has been shown to interact in vitro and in mammalian cells with a conserved BC-box motif found in a growing number of proteins including RNA polymerase II elongation factor Elongin A, SOCS-box proteins, and the von Hippel-Lindau (VHL) tumor suppressor protein [6].

Biological context of TCEB3

• To identify proteins that can bind to these conserved sequences, a human B cell cDNA library was screened using the NH(2)-terminus of Elongin A as bait in a yeast two-hybrid system [7].
• Identification of EloA-BP1, a novel Elongin A binding protein with an exonuclease homology domain [7].
• Assignment of a human gene encoding the 110-kDa subunit of general transcription factor elongin (SIII) to chromosome 1p36.1 [8].
• Changing the SIII sequence also led to decreased dimer formation, confirming its contribution to the dimerization process [9].
• The proportions of aneuploid tumors in each of the tumor stages SI, SII, SIII, and SIV were 47%, 62%, 67%, and 69%, respectively [10].

Anatomical context of TCEB3

• Double immunofluorescence labeling in COS7 cells suggested that EloA-BP1 and Elongin A are colocalized to the cell nucleus [7].
• Five somatosensory cortices have distinctive somatotopic representations, cytoarchitecture, and connectivity: primary somatosensory cortex (SI), ventrolateral association cortices (SII, SIII, and SIV), and dorsomedial association cortex (supplementary sensory area) [11].

Associations of TCEB3 with chemical compounds

• Furthermore, SI and SIII preferentially repressed the heterologous thymidine kinase and homologous DBH proximal promoter activities in nonneuronal cells [12].
• For NaX, the SIII' cations which occupy the most accessible adsorption sites are significantly moving upon coordination to the methanol molecules; the extent of this mobility exhibits a maximum for 48 methanol molecules per unit cell before decreasing at higher loadings due to steric hindrance [13].
• The extraframework cation sites located in the vicinity of the double six-member rings (D6R) of FAU zeolites (SI, SI', SIII') were considered and clusters with composition (M(n)(+))(2/)(n)()H(12)Si(10)Al(2)O(18), M = Li(+), Na(+), K(+), Ca(2+), were selected to represent the adsorption centers [14].
• We propose that the SIII sites may be a more likely location for methanol activation, particularly in the reaction with toluene, which favors the SII site [15].
• Solvates from 2-propanol (SII), trichloromethane (SIII) and tetrachloromethane (SIV) have been characterized [16].

Other interactions of TCEB3

• By using an in vitro binding assay, we show that EloA-BP1 is capable of binding not only the NH(2)-terminal approximately 120 amino acid region of Elongin A, but also that of SII [7].
• Structure-function analyses using fusion proteins composed of Elongin A3 and Elongin A revealed that the COOH-terminal region of Elongin A is important for the activation by Elongin BC [17].
• To further understand the role of Elongin A in transcriptional regulation by RNA polymerase II, we are attempting to identify Elongin A-related proteins [17].
• Here, we report on the cloning, expression, and characterization of human Elongin A2, a novel transcription elongation factor that exhibited 47% identity and 61% similarity to Elongin A [18].
• Domain I is conserved in evolution from yeast to human species and is homologous to the transcription factors elongin A and CRSP70 [19].

Analytical, diagnostic and therapeutic context of TCEB3

• In contrast, constructs containing mutations in SI and SIII replicated to some extent in cell culture after an initial drop in viral replication [9].

References