http://purl.uniprot.org/citations/32708832 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/32708832 | http://www.w3.org/2000/01/rdf-schema#comment | "Yeast prions and mnemons are respectively transmissible and non-transmissible self-perpetuating protein assemblies, frequently based on cross-β ordered detergent-resistant aggregates (amyloids). Prions cause devastating diseases in mammals and control heritable traits in yeast. It was shown that the de novo formation of the prion form [PSI+] of yeast release factor Sup35 is facilitated by aggregates of other proteins. Here we explore the mechanism of the promotion of [PSI+] formation by Ste18, an evolutionarily conserved gamma subunit of a G-protein coupled receptor, a key player in responses to extracellular stimuli. Ste18 forms detergent-resistant aggregates, some of which are colocalized with de novo generated Sup35 aggregates. Membrane association of Ste18 is required for both Ste18 aggregation and [PSI+] induction, while functional interactions involved in signal transduction are not essential for these processes. This emphasizes the significance of a specific location for the nucleation of protein aggregation. In contrast to typical prions, Ste18 aggregates do not show a pattern of heritability. Our finding that Ste18 levels are regulated by the ubiquitin-proteasome system, in conjunction with the previously reported increase in Ste18 levels upon the exposure to mating pheromone, suggests that the concentration-dependent Ste18 aggregation may mediate a mnemon-like response to physiological stimuli."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.org/dc/terms/identifier | "doi:10.3390/ijms21145038"xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Yang Z."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Karpova T.S."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Wilkinson K.D."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Chernova T.A."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Chernoff Y.O."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Shanks J.R."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/author | "Shcherbik N."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/name | "Int J Mol Sci"xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/pages | "E5038"xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/title | "Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association."xsd:string |
http://purl.uniprot.org/citations/32708832 | http://purl.uniprot.org/core/volume | "21"xsd:string |
http://purl.uniprot.org/citations/32708832 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32708832 |
http://purl.uniprot.org/citations/32708832 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32708832 |
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http://purl.uniprot.org/uniprot/A0A6A5PT44 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32708832 |
http://purl.uniprot.org/uniprot/P18852 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32708832 |