El Institut Universitari de Biotecnologia i Biomedicina (BIOTECMED) organiza una nueva charla el viernes 13 de junio a las 9:45 h en el aula AI-16A del aulario interfacultivo. Vanesa Bernal, del grupo EGE-DtoP, presentará la conferencia titulada Proteostasis control by eIF5A in health and disease.
El próximo viernes 13 de junio, a las 9:45h, se celebrará una nueva charla del Institut Universitari de Biotecnologia i Biomedicina (BIOTECMED), que en esta ocasión correrá a cargo de Vanesa Bernal, investigadora del grupo EGE-DtoP. Su ponencia lleva por título Proteostasis control by eIF5A in health and disease y abordará el papel fundamental de la proteína eIF5A en el control de la proteostasis y su implicación en diversas enfermedades. La charla tendrá lugar en el aula AI-16A del aulario interfacultatiu.
Este estudio investiga el papel esencial de la proteína eIF5A en la traducción de ARNm, especialmente durante el estrés térmico en la levadura Saccharomyces cerevisiae. Se demuestra que eIF5A es crucial para la síntesis de chaperonas necesarias para mantener la homeostasis proteica, y su ausencia causa sensibilidad al calor, fallos en mecanismos de defensa celular y acumulación de proteínas mal plegadas. La investigación resalta su importancia en evitar agregados proteicos relacionados con enfermedades humanas como el Huntington.
Abstract de la charla:
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).
