Conserved mechanism of Xrn1 regulation by glycolytic flux and protein aggregation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378041%3A_____%2F25%3A00603114" target="_blank" >RIV/68378041:_____/25:00603114 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Conserved mechanism of Xrn1 regulation by glycolytic flux and protein aggregation
Original language description
Gene expression in eukaryotes is largely controlled by exoribonucleases that degrade decapped mRNAs in the 5’–3’ direction. Xrn1, the major yeast exoribonuclease, is regulated through changes in cellular localization linked to metabolic state. Under fermentable carbon conditions, Xrn1 is active in the cytosol, while carbon depletion leads to its sequestration at eisosomes and inactivation. We show that Xrn1 membrane binding depends on glycolytic flux rather than carbon source availability, is independent of TORC1, and requires Pil1 and Lsp1. The SH3-like domain of Xrn1 likely mediates this interaction. Notably, the human Xrn1 orthologue expressed in yeast shows similar behavior, localizing to eisosomes when glycolysis is halted. These findings reveal a conserved regulatory mechanism from yeast to humans.
Czech name
—
Czech description
—

Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)