FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2947790762> ?p ?o ?g. }

• W2947790762 endingPage "771" @default.
• W2947790762 startingPage "757" @default.
• W2947790762 abstract "Abstract Self-perpetuating protein aggregates (prions) cause diseases in mammals. Yeast prions are heritable in cell divisions. Howie et al. demonstrate that the cellular apparatus responsible for the asymmetry of cell division controls destabilization of a yeast prion... Self-perpetuating transmissible protein aggregates, termed prions, are implicated in mammalian diseases and control phenotypically detectable traits in Saccharomyces cerevisiae. Yeast stress-inducible chaperone proteins, including Hsp104 and Hsp70-Ssa that counteract cytotoxic protein aggregation, also control prion propagation. Stress-damaged proteins that are not disaggregated by chaperones are cleared from daughter cells via mother-specific asymmetric segregation in cell divisions following heat shock. Short-term mild heat stress destabilizes [PSI+], a prion isoform of the yeast translation termination factor Sup35. This destabilization is linked to the induction of the Hsp104 chaperone. Here, we show that the region of Hsp104 known to be required for curing by artificially overproduced Hsp104 is also required for heat-shock-mediated [PSI+] destabilization. Moreover, deletion of the SIR2 gene, coding for a deacetylase crucial for asymmetric segregation of heat-damaged proteins, also counteracts heat-shock-mediated destabilization of [PSI+], and Sup35 aggregates are colocalized with aggregates of heat-damaged proteins marked by Hsp104-GFP. These results support the role of asymmetric segregation in prion destabilization. Finally, we show that depletion of the heat-shock noninducible ribosome-associated chaperone Hsp70-Ssb decreases heat-shock-mediated destabilization of [PSI+], while disruption of a cochaperone complex mediating the binding of Hsp70-Ssb to the ribosome increases prion loss. Our data indicate that Hsp70-Ssb relocates from the ribosome to the cytosol during heat stress. Cytosolic Hsp70-Ssb has been shown to antagonize the function of Hsp70-Ssa in prion propagation, which explains the Hsp70-Ssb effect on prion destabilization by heat shock. This result uncovers the stress-related role of a stress noninducible chaperone." @default.
• W2947790762 created "2019-06-07" @default.
• W2947790762 creator A5038113781 @default.
• W2947790762 creator A5048669656 @default.
• W2947790762 creator A5060215089 @default.
• W2947790762 creator A5061172312 @default.
• W2947790762 creator A5061335787 @default.
• W2947790762 creator A5077823225 @default.
• W2947790762 creator A5082912822 @default.
• W2947790762 creator A5087527715 @default.
• W2947790762 date "2019-06-13" @default.
• W2947790762 modified "2023-10-14" @default.
• W2947790762 title "Role of the Cell Asymmetry Apparatus and Ribosome-Associated Chaperones in the Destabilization of a <i>Saccharomyces cerevisiae</i> Prion by Heat Shock" @default.
• W2947790762 cites W1222091784 @default.
• W2947790762 cites W1497947649 @default.
• W2947790762 cites W1616900398 @default.
• W2947790762 cites W1857855090 @default.
• W2947790762 cites W1894729831 @default.
• W2947790762 cites W1962225963 @default.
• W2947790762 cites W1966072209 @default.
• W2947790762 cites W1977796112 @default.
• W2947790762 cites W1988561224 @default.
• W2947790762 cites W1990365848 @default.
• W2947790762 cites W1993698518 @default.
• W2947790762 cites W2000204824 @default.
• W2947790762 cites W2005369928 @default.
• W2947790762 cites W2008217034 @default.
• W2947790762 cites W2027156371 @default.
• W2947790762 cites W2036404841 @default.
• W2947790762 cites W2044061340 @default.
• W2947790762 cites W2046756800 @default.
• W2947790762 cites W2054393791 @default.
• W2947790762 cites W2056452325 @default.
• W2947790762 cites W2057505896 @default.
• W2947790762 cites W2059277971 @default.
• W2947790762 cites W2060303895 @default.
• W2947790762 cites W2065579794 @default.
• W2947790762 cites W2072455244 @default.
• W2947790762 cites W2079825405 @default.
• W2947790762 cites W2086660631 @default.
• W2947790762 cites W2092587339 @default.
• W2947790762 cites W2098898403 @default.
• W2947790762 cites W2105375182 @default.
• W2947790762 cites W2111574701 @default.
• W2947790762 cites W2118360452 @default.
• W2947790762 cites W2122070718 @default.
• W2947790762 cites W2124258182 @default.
• W2947790762 cites W2124466665 @default.
• W2947790762 cites W2127157203 @default.
• W2947790762 cites W2135532366 @default.
• W2947790762 cites W2136679442 @default.
• W2947790762 cites W2138375704 @default.
• W2947790762 cites W2150555206 @default.
• W2947790762 cites W2162179975 @default.
• W2947790762 cites W2167990179 @default.
• W2947790762 cites W2169665392 @default.
• W2947790762 cites W2189788457 @default.
• W2947790762 cites W2296137721 @default.
• W2947790762 cites W2332526708 @default.
• W2947790762 cites W2547881573 @default.
• W2947790762 cites W2567962298 @default.
• W2947790762 cites W2577386528 @default.
• W2947790762 cites W2604251699 @default.
• W2947790762 cites W2605851660 @default.
• W2947790762 cites W2615647870 @default.
• W2947790762 cites W2755917570 @default.
• W2947790762 cites W2762551856 @default.
• W2947790762 cites W2772823592 @default.
• W2947790762 cites W2796861680 @default.
• W2947790762 cites W2802046579 @default.
• W2947790762 doi "https://doi.org/10.1534/genetics.119.302237" @default.
• W2947790762 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6614889" @default.
• W2947790762 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33954397" @default.
• W2947790762 hasPublicationYear "2019" @default.
• W2947790762 type Work @default.
• W2947790762 sameAs 2947790762 @default.
• W2947790762 citedByCount "9" @default.
• W2947790762 countsByYear W29477907622019 @default.
• W2947790762 countsByYear W29477907622020 @default.
• W2947790762 countsByYear W29477907622021 @default.
• W2947790762 countsByYear W29477907622022 @default.
• W2947790762 countsByYear W29477907622023 @default.
• W2947790762 crossrefType "journal-article" @default.
• W2947790762 hasAuthorship W2947790762A5038113781 @default.
• W2947790762 hasAuthorship W2947790762A5048669656 @default.
• W2947790762 hasAuthorship W2947790762A5060215089 @default.
• W2947790762 hasAuthorship W2947790762A5061172312 @default.
• W2947790762 hasAuthorship W2947790762A5061335787 @default.
• W2947790762 hasAuthorship W2947790762A5077823225 @default.
• W2947790762 hasAuthorship W2947790762A5082912822 @default.
• W2947790762 hasAuthorship W2947790762A5087527715 @default.
• W2947790762 hasBestOaLocation W29477907621 @default.
• W2947790762 hasConcept C104317684 @default.
• W2947790762 hasConcept C105580179 @default.
• W2947790762 hasConcept C117838200 @default.
• W2947790762 hasConcept C136238340 @default.
• W2947790762 hasConcept C137984847 @default.
• W2947790762 hasConcept C142724271 @default.

• next