{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T07:54:56Z","timestamp":1791446096366,"version":"4.3.3"},"reference-count":72,"publisher":"Shared Science Publishers OG","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"Abstract<\/jats:title>\n \n Protein misfolding and aberrant protein aggregation are central features of neurodegenerative disorders, including amyotrophic lateral sclerosis, where the RNA-binding protein TDP-43 accumulates in abnormal intracellular assemblies. Although yeast models have identified multiple modifiers of TDP-43 toxicity, the cellular factors that determine how aggregation-prone proteins are organized remain incompletely understood. Here, we investigated whether the ribosome- and mRNP-associated proteins Scp160 and Bfr1 influence TDP-43 proteotoxicity and aggregate formation. We report that deletion of\n SCP160<\/jats:italic>\n or\n BFR1<\/jats:italic>\n improves growth during TDP43-GFP induction without reducing steady-state reporter abundance and decreases formation of prominent TDP43-GFP foci. Deletion of\n BFR1<\/jats:italic>\n produced an intermediate TDP-43 phenotype, with a weaker effect than\n SCP160<\/jats:italic>\n deletion on severe foci formation and toxicity. Importantly, the effect of\n SCP160<\/jats:italic>\n or\n BFR1<\/jats:italic>\n deletion on visible protein aggregation was not specific to TDP-43: severe Htt103Q-GFP aggregation was strongly reduced, and formation of VHL-GFP foci was suppressed, including under conditions of proteasome inhibition. Despite these shared effects, the two mutants were not phenotypically identical. Deletion of\n SCP160<\/jats:italic>\n produced a distinct spatial phenotype in which residual TDP43-GFP foci showed markedly increased association with Sec63-positive ER structures and reduced distance to these regions, whereas\n bfr1<\/jats:italic>\n \n \n \u0394<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n cells did not show the same Sec63-associated shift. Together, these findings uncouple TDP43-GFP abundance from toxicity and prominent foci formation and identify Scp160 and Bfr1 as factors that influence the intracellular partitioning of aggregation-prone and misfolded proteins, with an additional role for Scp160 in the spatial organization of TDP43 relative to the ER.\n <\/jats:p>","DOI":"10.15698\/mic2026.10.888","type":"journal-article","created":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T07:26:16Z","timestamp":1791444376000},"page":"358-377","source":"Crossref","is-referenced-by-count":0,"title":["Scp160 deletion suppresses TDP-43 aggregation and toxicity in Saccharomyces cerevisiae"],"prefix":"10.15698","volume":"13","author":[{"given":"Joan","family":"Castells-Ballester","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Shcherbik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"6394","published-online":{"date-parts":[[2026,10,6]]},"reference":[{"key":"b011c8","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu Rev Biochem"},{"issue":"10","key":"b0122b","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41593-018-0235-9","article-title":"Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases","volume":"21","author":"Soto","year":"2018","journal-title":"Nat 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