Disease relevance of eIF-4E

• Structural analysis of the eukaryotic initiation factor 4E gene controlling potyvirus resistance in pepper: exploitation of a BAC library [1].
• The CBP tag produced moderate purity protein from E. coli, yeast, and Drosophila extracts, but better purity from HeLa extracts [2].

High impact information on eIF-4E

• A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP [3].
• Genetic models of junctional plasticity and genetic manipulations using the translation initiation factors eIF4E and poly(A)-binding protein showed an increased occurrence of subsynaptic translation aggregates [4].
• We show that translational repression of cad mRNA is dependent on a functional eIF4E-binding motif [5].
• Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome [6].
• We demonstrate that acetylation of HMG I(Y) by CBP is essential for turning off IFN beta gene expression [6].

Biological context of eIF-4E

• These results, together with genetic epistasis studies, suggest that postsynaptic Pum modulates synaptic function via direct control of eIF-4E expression [7].
• Drosophila melanogaster contains a single copy of the gene encoding translation eukaryotic initiation factor eIF-4E, which maps in the 67A2B1 region of chromosome 3L [8].
• The third mRNA species contains a new open reading frame, possibly encoding another isoform of eIF-4E, which is very similar in size to the other but has a different N-terminal sequence [8].
• Expression of the eIF-4E gene is spatially and temporally controlled during embryonic development [8].
• Several sequences which may be involved in the regulation of transcription initiation of the eIF-4E gene, except for a consensus TATA box, were found upstream of the putative transcription initiation sites [8].

Anatomical context of eIF-4E

• As shown previously for eIF-4E, the p200 subunit was also required for the translation of endogenous mRNAs in cell-free systems from Drosophila embryos [9].
• Maskin contains a peptide sequence conserved among eIF-4E binding proteins that is involved in oocyte development [10].
• Polyclonal antibodies against Drosophila 35-kDa CBP neither reacted with eucaryotic initiation factor 4E from rabbit reticulocytes nor affected mRNA translation in a rabbit reticulocyte cell-free system [11].

Associations of eIF-4E with chemical compounds

• We show that CBP and P/CAF acetylate HMG I(Y), the essential architectural component required for enhanceosome assembly, at distinct lysine residues, causing distinct effects on transcription [6].
• Carotenoid-binding protein (CBP) from the silkworm Bombyx mori is an essential molecule for carotenoid dependent cocoon pigmentation [12].
• This study implies that alternative splicing of the BmStart1/CBP gene generates unique protein isoforms whose endogenous ligands, sterol or carotenoid, are structurally different [12].

Regulatory relationships of eIF-4E

• The translational repressor Pumilio regulates presynaptic morphology and controls postsynaptic accumulation of translation factor eIF-4E [7].
• Drosophila Lk6 kinase controls phosphorylation of eukaryotic translation initiation factor 4E and promotes normal growth and development [13].

Other interactions of eIF-4E

• Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression [14].
• One is Lk6, which encodes a protein kinase predicted to regulate the rate-limiting initiation factor eIF4E [15].
• Heat shock effects on phosphorylation of protein synthesis initiation factor proteins eIF-4E and eIF-2 alpha in Drosophila [16].

Analytical, diagnostic and therapeutic context of eIF-4E

• Genomic sequence analysis revealed that BmStart1 and CBP are generated from the same gene locus by alternative splicing [12].

References