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Stress-induced nucleocytoplasmic shuttling of TDP-43 is controlled by eIF-5A hypusination
Poster Title: Stress-induced nucleocytoplasmic shuttling of TDP-43 is controlled by eIF-5A hypusination
Submitted on 10 Feb 2017
Author(s): Carlos Osorno, Shayna Smeltzer, Frank Zamudio, Zain Quadri, Maj-Linda Selenica
Affiliations: Byrd Alzheimers Institute
This poster was presented at USF Health Research Day 2017
Poster Views: 1,042
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Poster Information
Abstract: Aggregation and phosphorylation of TAR DNA-binding protein-43, TDP-43, has been found to be associated with the neuropathology of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTLD). It has been proposed that TDP-43 accumulation in stress granules (SG) may contribute to the aggregation of TDP43. Eukaryotic translational initiation factor 5A (eIF5A) is hypusinated by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). It is involved at the level of mRNA turnover, cell proliferation, and protein translational elongation. In this experiment we sought to determine the function of hypusinated eIF5a in relation to TDP-43 pathology in nuclear and cytoplasmic compartments under cellular stress. Summary: An optimal concentration of GC7 and tetracycline was discovered. Additionally, by inhibiting hypusination of eIF-5A, TDP-43 nucleocytoplasmic shuttling and stress granule formation was reduced.Report abuse »
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