Stress-induced nucleocytoplasmic shuttling of TDP-43 is controlled by eIF-5A hypusination
Poster Feb 13, 2017
Carlos Osorno, Shayna Smeltzer, Frank Zamudio, Zain Quadri, Maj-Linda Selenica
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.
www.thebraindomain.org: Science Writing for Public EngagementPoster
The Brain Domain is a blog and article focused public engagement website, geared towards helping young neuroscientists improve their skills in science writing and communication.READ MORE
MEG Resting State Functional Connectivity and Network Topology in Dyslexia Related GenotypePoster
Studying resting state neuro-functional interactions and their network distribution may tell us more about differences in typical and a typical brain development.
Analysis of the Effect of Aggregated β-Amyloid on Cellular Signaling Pathways Critical for Memory in Alzheimer’s DiseasePoster
Here we evaluate the ability to detect changes in phosphorylation levels of ERK and CREB following treatment with Aβ using the SH-SY5Y neuroblastoma cell line.READ MORE