Disease relevance of EEF1D

• We demonstrate that gain of 8q and expression levels of three 8q-mapped candidate genes (EEF1D, RPL30, RPS20) are associated with adverse outcome in medulloblastoma [1].
• Here we show that four proteins, namely the translationally controlled tumor protein, the human elongation factor 1-delta, tetratricopeptide repeat protein and the isoform 14-3-3-gamma of the 14-3-3-family are overexpressed in chemoresistant melanoma cell lines [2].
• A higher expression of EF-1 delta was significantly correlated with lymph node metastases (P<0.05) and advanced stages (P<0.05) [3].
• Here, we report that the human translation elongation factor 1-delta (EF-1 delta) binds to the second exon of HIV-1 Tat [4].

High impact information on EEF1D

• Cell cycle analysis shows that EF-1 delta expression enhancement precedes G2 arrest in these cells, suggesting that EF-1 delta may participate in the G2-M cell cycle checkpoint [5].
• The minimal EF-1 delta-binding domain on kinectin resides within a conserved region present in all the kinectin isoforms [6].
• EF-1 delta provides the guanine nucleotide exchange activities on EF-1 alpha during elongation step of protein synthesis [6].
• Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum [6].
• The results demonstrate that the NH2-terminal extension of valyl-tRNA synthetase is required for complex formation and that the enzyme-binding site(s) resides on the EF-1 delta subunit [7].

Biological context of EEF1D

• Medulloblastoma outcome is adversely associated with overexpression of EEF1D, RPL30, and RPS20 on the long arm of chromosome 8 [1].
• Phosphorylation studies revealed the presence of two post-translational regulated forms of EF-1 delta protein [8].
• To explore the relation between oncogenes and EF-1 delta expression, a variety of oncogenes were introduced into human mammary epithelial cells (MCF-7) and human keratinocytes (HaCaT) [9].
• The higher expression of EF-1 delta in the tumours suggested that malignant transformation in vivo requires an increase in translation factor mRNA and protein synthesis for entry into and transition through the cell cycle [9].
• To explore the relation between cell division and EF-1 delta expression, MCF-7 cells were treated with dexamethasone, an inducer of differentiation [9].

Anatomical context of EEF1D

• Elongation factor EF-1 delta, a new target for maturation-promoting factor in Xenopus oocytes [8].
• EF-1 delta mRNA is present as a single 2.7-kb transcript in unfertilized eggs and in rapidly dividing cleavage stage embryos [10].
• Since the 2.0-kb polyadenylated form of the EF-1 delta transcript appears at gastrula stage, our results suggest that a mechanism for alternative poly(A) site selection of the EF-1 delta transcript appears during embryonic development [10].
• Four of the identified proteins were differentially phosphorylated: annexin-1, an actin-binding protein and a substrate for receptor tyrosine kinases; tropomyosin-alpha, a regulator of actin filament stability and cell shape; elongation factor 1 delta; ATP synthase beta-chain [11].

Associations of EEF1D with chemical compounds

• EF-1 delta is phosphorylated by Cdc2 kinase on threonine and serine residues [8].
• There was no change in the mRNA levels of EF-1 delta in the dexamethasone-treated cells [9].

Other interactions of EEF1D

• Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation [7].
• Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta) [12].
• This report provides evidence of an alternative kinectin function as the membrane anchor for EF-1 delta on the endoplasmic reticulum and provides clues to the EF-1 complex assembly and anchorage on the endoplasmic reticulum [6].
• In this report, we demonstrate that three components of EF-1H (EF-1 beta, EF-1 delta, EF-1 gamma) bind to DNA modified with chromium (Cr), a potent DNA-damaging agent and an established human carcinogen [13].
• Despite high oncogene mRNA expression, there was no significant change in the EF-1 delta mRNA level by v-src, c-erbB (EGF Receptor), c-erbB-2, v-myc and v-fos oncogenes [9].

References