ArticleMolecular cell2018
SRCP1 Conveys Resistance to Polyglutamine Aggregation.
Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum.BMC molecular and cell biology · 2026Article
- Viral vector gene delivery of the novel chaperone protein SRCP1 to modify insoluble protein in in vitro and in vivo models of ALS.Gene therapy · 2023Article
- Mechanistic Insight into the Suppression of Polyglutamine Aggregation by SRCP1.ACS chemical biology · 2023Article
- Insights on Microsatellite Characteristics, Evolution, and Function From the Social AmoebaFrontiers in neuroscience · 2022Review
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- RACK1 modulates polyglutamine-induced neurodegeneration by promoting ERK degradation in Drosophila.PLoS genetics · 2021Article
- Review
- Development of a Positive Selection High Throughput Genetic Screen inFrontiers in cell and developmental biology · 2021Article
- Assessing the necessity of a family of genes that encode small proteins inmicroPublication biology · 2021Article
- Eukaryotic life without tQCUG: the role of Elongator-dependent tRNA modifications in Dictyostelium discoideum.Nucleic acids research · 2020Article
- Amino acid homorepeats in proteins.Nature reviews. Chemistry · 2020Review
- Pathogenesis of SCA3 and implications for other polyglutamine diseases.Neurobiology of disease · 2020Review
- A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during Dictyostelium discoideum Development.mSphere · 2019Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The polyglutamine (polyQ) diseases are a group of nine neurodegenerative diseases caused by the expansion of a polyQ tract that results in protein aggregation. Unlike other model organisms, Dictyostelium discoideum is a proteostatic outlier, naturally encoding long polyQ tracts yet resistant to polyQ aggregation. Here we identify serine-rich chaperone protein 1 (SRCP1) as a molecular chaperone that is necessary and sufficient to suppress polyQ aggregation. SRCP1 inhibits aggregation of polyQ-expanded proteins, allowing for their degradation via the proteasome, where SRCP1 is also degraded. SRCP1's C-terminal domain is essential for its activity in cells, and peptides that mimic this domain suppress polyQ aggregation in vitro. Together our results identify a novel type of molecular chaperone and reveal how nature has dealt with the problem of polyQ aggregation.
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Registered trials
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