Pregled bibliografske jedinice broj: 1199148
Characterization of human tau protein in yeast cells
Characterization of human tau protein in yeast cells // COST Action 20113 ProteoCure / Auf dem Keller, Ulrich (ur.).
Ljubljana, 2022. str. 1-1 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 1199148 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Characterization of human tau protein in yeast cells
(Characterization of human Tau protein in yeast cells)
Autori
Zubčić, Klara ; Franić, Dina ; Pravica, Mihaela ; Renić, Marija ; Bedalov, Antonio ; Šimić, Goran ; Boban, Mirta
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
COST Action 20113 ProteoCure
/ Auf dem Keller, Ulrich - Ljubljana, 2022, 1-1
Skup
ProteoCure COST Meeting
Mjesto i datum
Ljubljana, Slovenija, 17.05.2022. - 19.05.2022
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aging ; Alzheimer’s disease ; protein aggregation ; protein homeostasis ; tau gene ; tau protein
Sažetak
Age-dependent protein aggregation is a conserved phenomenon that is associated with many neurodegenerative diseases, including Alzheimer's disease (AD). AD is characterized by aggregation of Tau, a microtubule-binding protein that is normally soluble and mainly localized to neuronal axons, but which can form oligomers and higher order amyloid-like aggregates that accumulate in soma and dendrites and eventually lead to neuronal death. Although the main risk factor for the onset of AD is aging, the exact causes of Tau protein aggregation are still largely unclear. To investigate factors that influence Tau protein aggregation, we expressed human Tau protein fused with fluorescent proteins in yeast Saccharomyces cerevisiae. We examined the intracellular localization of Tau in young and aged cells, and in cells under different stress conditions, such as glucose starvation, hyperosmotic stress, elevated temperature and proteotoxic stress caused by a toxic amino acid analogue. Furthermore, to study the factors affecting Tau oligomerization, which is considered to be an early step in Tau pathology, we used luminescent reporter NanoBiT in which protein-protein interaction results in the complementation of the luciferase NanoLuc. Our results show basal levels of Tau-NanoBiT reporter signal in logarithmically growing wild-type cells, suggesting that Tau oligomerization does not occur under normal growth conditions.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Temeljne medicinske znanosti, Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)
POVEZANOST RADA
Ustanove:
Medicinski fakultet, Zagreb
Profili:
Klara Zubčić
(autor)
Goran Šimić
(autor)
Dina Franić
(autor)
Marija Renić
(autor)
Mirta Boban
(autor)