The University Institute of Biotechnology and Biomedicine (BIOTECMED) is organizing a new talk on Friday, June 13 at 9:45 a.m. in classroom AI-16A (interfaculty building). Vanesa Bernal, from the EGE-DtoP group, will deliver a lecture titled Proteostasis control by eIF5A in health and disease.

On Friday, June 13 at 9:45 a.m., a new talk will be held by the University Institute of Biotechnology and Biomedicine (BIOTECMED), presented by Vanesa Bernal, a researcher from the EGE-DtoP group. Her lecture, titled Proteostasis control by eIF5A in health and disease, will address the fundamental role of the eIF5A protein in the regulation of proteostasis and its implications in various diseases. The talk will take place in classroom AI-16A of the interfaculty building.

This study investigates the essential role of the eIF5A protein in mRNA translation, especially under heat stress in the yeast Saccharomyces cerevisiae. The findings demonstrate that eIF5A is crucial for the synthesis of chaperone proteins necessary to maintain protein homeostasis. Its absence leads to heat sensitivity, failures in cellular defense mechanisms, and accumulation of misfolded proteins. The research highlights its importance in preventing protein aggregates linked to human diseases such as Huntington’s.

Abstract of the talk:

The translation of mRNA into polypeptides is one of the most fundamental biological processes, affected by multiple factors. eIF5A is an essential, abundant and evolutionarily conserved protein, primarily acting as a translation elongation factor. This factor binds to ribosomes, facilitating the translation of specific peptide motifs by assisting stalled ribosomes to promote elongation and it has been linked to various diseases, including cancer, viral infections, diabetes, neurodevelopmental disorders and aging. During heat stress and aging, chaperones are essential for maintaining cellular proteostasis. Our studies in the yeast Saccharomyces cerevisiae indicate that eIF5A protein levels increase at high temperatures, whereas its depletion leads to heat sensitivity. A lack of eIF5A impairs stress-resistance mechanisms, such as translation arrest and the formation of stress granules and P-bodies. Notably, eIF5A depletion results in the defective translation of mRNA encoding chaperones, particularly Hsp70, Hsp100, and small heat shock proteins. However, the dependency of these chaperones on eIF5A does not appear to be related to the presence of specific eIF5A-dependent peptide motifs in their sequences. Instead, it seems to be related to other specific characteristics of their mRNAs. Our results demonstrate that the absence of chaperone synthesis in eIF5A-depleted cells results in issues with protein homeostasis, highlighting the pivotal role of eIF5A in preventing the formation of protein aggregates associated with human proteopathies, such as Huntington's disease (HD).