High impact information on EIF3S12

• The presence of distinct binding sites for rpL23a and the M9 import signal in transportin, and for rpL23a and importin alpha in importin beta might explain how a single receptor can recognize very different import signals [1].
• We have found that a segment of ca. 40 amino acids near the carboxyl end of the protein (designated M9) is necessary and sufficient for nuclear localization; attaching this segment to the bacterial protein beta-galactosidase or to pyruvate kinase completely localized these otherwise cytoplasmic proteins to the nucleus [2].
• Arg134 and Arg133 lie on the surface of the catalytic subunit with Arg133 coming close to the amphipathic helix of PKI(5-24) (Knighton, D. R., Zheng, J., Ten Eyck, L. F., Xuong, N.-h., Taylor, S. S., and Sowadski, J. M. (1991) Science 253, 414-420) [3].
• We next introduced the Arg134-to-Ala and/or the Phe125-to-Ala mutation into the Ebola virus genome [4].
• The structural analysis at atomic resolution reveals that residue Arg134 (alphaA2), which interacts with the phosphotyrosine side-chain, is present in two conformations in the complex [5].

Biological context of EIF3S12

• Sequences homologous with eIF3k are found in the genomes of Caenorhabitis elegans, Arabidopsis thaliana and Drosophila melanogaster, and a homologous protein has been reported to be present in wheat eIF3 [6].
• The fast dispersion of the CTX-M-9 enzyme could therefore be due to both diffusion of plasmids and mobile elements [7].
• To characterize this SLC-specific antigen further, a spleen cDNA library established in the expression vector lambda gt-11 was searched immunochemically for clones expressing the Ki-M9 antigen [8].
• The M9 nuclear shuttle peptide consistently increased the transfection efficiency [9].
• Four blood samples were sent to the laboratories, to be analysed for 11 Y-chromosome single nucleotide polymorphisms (SNPs): SRY-1532, M40, M35, M213, M9, 92R7, M17, P25, M18, M153 and M167 [10].

Anatomical context of EIF3S12

• These observations suggest that PLAC-24 may play a role in the transport and the stabilisation of newly synthesised 5-HT(7) receptor towards the plasma membrane [11].
• The association of PLAC-24 with all three receptor variants was observed and further reconfirmed in vivo by co-immunoprecipitation of PLAC-24 with the full-length receptor isoforms in transfected COS-7 cells [11].
• Human sinus-lining cells (SLC) of the lymph node sinuses most probably represent accessory cells for the primary humoral immune response and have been shown to express a unique antigen recognized by the monoclonal antibody Ki-M9 [8].
• In this study, the long-term effects of infection by the avirulent M9 mutant of SPV on the central nervous system (CNS) of BALB/c and SJL mice were determined [12].
• Cloning of a complementary DNA encoding the unique dendritic cell antigen Ki-M9 [8].

Associations of EIF3S12 with chemical compounds

• The only arginine side-chain built into good density is that of Arg134 at the extracellular end of helix E, the others being disordered near one of the two surfaces [13].
• Fluorescent microscopy demonstrated that the M9 shuttle allowed rhodamine-tagged plasmid to gain access to the nucleus, while it was located exclusively in the cytoplasm without the peptide [9].

Physical interactions of EIF3S12

• We found that cyclin D3 specifically interacted with eIF3k through its C-terminal domain [14].
• A monoclonal anti-eIF3a (p170) Ig coimmunoprecipitates eIF3k with the eIF3 complex [6].

Co-localisations of EIF3S12

• Immunofluorescence experiments showed that eIF3k distributed both in nucleus and cytoplasm and colocalized with cyclin D3 [14].

Other interactions of EIF3S12

• The association of cyclin D3 with eIF3k was further confirmed by in vitro binding assay, in vivo coimmunoprecipitation, and confocal microscopic analysis [14].

Analytical, diagnostic and therapeutic context of EIF3S12

• Using a yeast two-hybrid assay, we isolated PLAC-24/eIF3k as a possible interacting candidate [11].
• By applying non-radioactive in situ hybridization on mouse tissue, strong expression in SLC of the lymph node and metallophilic cells of the spleen in mouse tissue could be seen indicating that the Ki-M9 cDNA is highly conserved in the two species [8].
• The M9 shuttle peptide increases transfection efficiency in esophageal mucosal cells, and therefore may have a useful role in gene therapy applications involving the esophagus [9].

References