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Results describe the identification and characterization of nero, the Drosophila melanogaster deoxyhypusine hydroxylase (DOHH) homologue, and indicate that nero and eIF5A are required for cell growth and affect autophagy and protein synthesis.
phosphorylation of Ser(2) plays a role in regulation of nucleocytoplasmic shuttling of eIF5A in plant cells
Findings indicate that eIF5A (show EIF5 Proteins)-PEAK1 (show PEAK1 Proteins)-YAP (show YAP1 Proteins) signaling contributes to PDAC development by regulating an STF program associated with increased tumorigenicity.
eIF5A1 isoform A has a role in mitochondrial function.
These results suggest that binding of eEF2 (show EEF2 Proteins) to the ribosome alters its conformation, resulting in a weakened affinity of eIF5A (show EIF5 Proteins) and impairment of this interplay compromises cell growth due to translation elongation defects.
eIF5A (show EIF5 Proteins)-2 protein was highly expressed in gastric cancer tissues
Upregulation of translation initiation factor 5a observed in thalassemia is a novel finding and plays a protective role toward cell survival under oxidative stress.
Our results suggest that functional, hypusinated eIF5A (show EIF5 Proteins) is necessary for HIF-1alpha (show HIF1A Proteins) expression during hypoxia and that eIF5A (show EIF5 Proteins) is an attractive target for cancer therapy.
findings also implicate the eIF5A (show EIF5 Proteins)/RhoA (show RHOA Proteins)/ROCK module as a potential new therapeutic target to treat metastatic PDAC cells
eIF5A (show EIF5 Proteins) has been shown to regulate a number of gene products specifically, termed the eIF5A (show EIF5 Proteins) regulon, and its role in translating proline-rich sequences has recently been identified.
eIF5A (show EIF5 Proteins) proteins utilize PEAK1 (show PEAK1 Proteins) as a downstream effector to drive pancreatic ductal adenocarcinoma (PDAC) pathogenesis.
Mature eIF5A (show EIF5 Proteins) (hypusinated form) is not involved in the autophagic pathway.
our results provide the first genetic evidence that the hypusine modification in eIF-5A is crucial for homeostasis in mammals
knockout of either the eIF5A-1 gene (Eif5a) or of the deoxyhypusine synthase (show DHPS Proteins) gene (Dhps (show DHPS Proteins)) caused early embryonic lethality in mice, indicating the essential nature of both eIF5A-1 and deoxyhypusine synthase (show DHPS Proteins) in mammalian development
These results point to a new functional role for eIF5A, relating it to embryogenesis, development, and cell differentiation.
a decrease in either active eIF5A or polyamines inhibits cell growth, indicating that eIF5A and polyamines are independently involved in cell growth
Results indicate that the N-terminal extension of the eukaryotic eIF5A contributes in signaling this protein to nuclear localization, despite of bearing no structural similarity with classical nuclear localization signals.
Eukaryotic initiation factor 5A (eIF5A) (eIF-4D, eIF-5A) stimulates ribosomal peptidyltransferase activity, transport of HIV-1-mRNAs and binds exportins 1 and 4. Contains hypusine at lys (show LYZ Proteins) 50. Mouse EIF5A1 and EIF5A2 (show EIF5A2 Proteins) encode two isoforms: eIF5AI and eIF5AII (show EIF5A2 Proteins).
The deduced bovine eIF5A protein is 100% identical to human Eif5A.
This gene encodes an elongation initiation factor, which participates in protein synthesis. The encoded protein also plays roles in mRNA metabolism, cell proliferation, and cell cycle control. This protein contains a modified lysine residue called hypusine, which appears to be necessary for its function. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 2, 5, and 19.
, eukaryotic initiation factor 5A
, eukaryotic translation factor 5A
, eukaryotic translation initiation factor 5A-1
, eukaryotic translation initiation factor 5A
, translation initiation factor 5A
, eukaryotic translation initiation factor 5a
, initiation factor 5a
, putative eukaryotic initiation factor 5a
, rev-binding factor