Disease relevance of EIF3S2

• Eukaryotic initiation factor 3 (eIF3) is involved in the initiation process of protein translation and overexpression of its subunit eukaryotic translation initiation factor i (eIF3i) has been observed in carcinomas [1].

High impact information on EIF3S2

• Moreover, we show that TRAP interacts with TRIP intracellularly, that activation of the TGFbeta type II receptor by TRIP-1 occurs in the presence of TRAP and that the differentiation process is mediated through the Smad2/3 pathway [2].
• Expression of other segments of TRIP-1 increased the TGF-beta-induced gene expression response and therefore may exert a dominant negative phenotype [3].
• Deletion mutational analysis revealed that two distinct regions, which do not contain recognizable WD40 repeats, are required for the ability of TRIP-1 to inhibit the gene expression response [3].
• The scandium dihydrosilyl complexes Cp*(2)ScSiH(2)R (R = Mes (4), Trip (5), SiPh(3) (6), Si(SiMe(3))(3) (7); Mes = 2,4,6-Me(3)C(6)H(2), Trip = 2,4,6-(i)()Pr(3)C(6)H(2)) and Cp*(2)ScSiH(SiMe(3))(2) (8) were synthesized by addition of the appropriate hydrosilane to Cp*(2)ScMe (1) [4].
• In contrast, 3 reacted with t-BuCN, 2,6-Trip(2)C(6)H(3)N(3) (Trip = 2,4,6-i-Pr(3)C(6)H(2)), and Ph(3)SiN(3) resulting in the displacement of the alkyne moiety to afford LAl[N(2)(Ct-Bu)(2)] (10) with an unprecedented aluminum-containing imidazole ring, and the first monomeric aluminum imides LAlNC(6)H(3)-2,6-Trip(2) (11) and LAlNSiPh(3) (12) [5].

Biological context of EIF3S2

• We have isolated the genomic sequence of TRIP-1 and found that the complete coding region is organised into 11 exons ranging from 39 to 397 bp and spanning approximately 9 kb of genomic DNA [6].
• Fluorescence in situ hybridisation mapped the TRIP-1 gene to chromosome 1p34.1 whereas a pseudogene is located on chromosome 7q32 [6].
• Thus, eIF3i overexpression fosters the integration of growth signals by mTOR into the mRNA translation process, promoting protein synthesis and tumor growth [1].
• Inhibition of the kinase mTOR, a key player in the integration of nutrition and growth signals into protein synthesis, with rapamycin reduced serine phosphorylation of eIF3i and resulted in a loss of anchorage-independent growth [1].
• Here, we show that in vitro overexpression of human eIF3i resulted in cell size increase, proliferation enhancement, cell-cycle progression, and anchorage-independent growth [1].

Associations of EIF3S2 with chemical compounds

• The lithium complexes Ar(C6H4-2-CH2NMe2)PLi undergo metathesis reactions with either NaOBut or KOBut to give the heavier alkali metal phosphides {Ar(C6H4-2-CH2NMe2)P}M.1/2OEt2 [Ar = mes, M = Na (8), K (9); Ar = Tripp, M = K (10)] [7].

Analytical, diagnostic and therapeutic context of EIF3S2

• Sequence analysis revealed that m56 is identical to mouse mSug1/FZA-B and shares high homology with human Trip1, moth 18-56, and yeast Sug1 [8].

References