Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies.
Ontology highlight
ABSTRACT: The yeast prion protein Sup35 is aggregation-prone at high concentrations. De novo Sup35 prion formation occurs at a significantly increased rate after transient overexpression of Sup35 in the presence of another prion, [PIN+], but it is still a rare event. Recent studies uncovered an additional and seemingly more prevalent role of Sup35: at its physiological level, it undergoes phase separation to form reversible condensates in response to transient stress. Stress-induced reversible Sup35 condensation in the [psi-] strain enhances cellular fitness after stress ceases, whereas irreversible Sup35 aggregates in the [PSI+] strain do not confer this advantage. However, how Sup35 overexpression, which could potentially lead to irrever
SUBMITTER: Feng J
PROVIDER: S-EPMC11921396 | biostudies-literature | 2025 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA