Naslov
A yeast model for studying human tau protein

Autori
Zubčić, Klara ; Franić, Dina ; Pravica, Mihaela ; Šimić, Goran ; Boban, Mirta

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
HDBMB22: From science to knowledge - Book of Abstracts / Dulić, Morana ; Sinčić, Nino ; Vrhovac Madunić, Ivana - Zagreb : Hrvatsko društvo za biokemiju i molekularnu biologiju (HDBMB), 2022, 161-161

Skup
Congress of the Croatian Society of Biochemistry and Molecular Biology: From Science to Knowledge (HDBMB22)

Mjesto i datum
Brela, Hrvatska, 28.09.2022. - 01.10.2022

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
aging ; Alzheimer's disease ; cell culture model ; glucose starvation ; hyperosmotic stress ; luminiscent reporter ; protein-protein interactions ; proteotoxic stress ; tau protein ; thermal stress ; yeast

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 its intracellular localization in young, logarithmically growing cells, in chronologically aged cells, and under different stress conditions, such as glucose starvation, hyperosmotic stress, elevated temperature, and proteotoxic stress caused by a toxic amino acid analog. 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, Kliničke medicinske znanosti, Kognitivna znanost (prirodne, tehničke, biomedicina i zdravstvo, društvene i humanističke znanosti), Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)

POVEZANOST RADA