ArticleMolecular biology of the cell2015
Autophagy protects against de novo formation of the [PSI+] prion in yeast.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
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- The Role of Cellular Prion Protein in Promoting Stemness and Differentiation in Cancer.Cancers · 2021Review
- Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020Review
- Review
- Crosstalk between Nrf2 signaling and mitochondrial function in Parkinson's disease.Molecular and cellular neurosciences · 2019Review
- The three faces of Sup35.Yeast (Chichester, England) · 2019Review
- Review
- Article
- Spermine increases acetylation of tubulins and facilitates autophagic degradation of prion aggregates.Scientific reports · 2018Article
- p62-Keap1-NRF2-ARE Pathway: A Contentious Player for Selective Targeting of Autophagy, Oxidative Stress and Mitochondrial Dysfunction in Prion Diseases.Frontiers in molecular neuroscience · 2018Review
- Regulation of MicroRNAs-Mediated Autophagic Flux: A New Regulatory Avenue for Neurodegenerative Diseases With Focus on Prion Diseases.Frontiers in aging neuroscience · 2018Review
- Induction of autophagy by spermidine is neuroprotective via inhibition of caspase 3-mediated Beclin 1 cleavage.Cell death & disease · 2017Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- The frequency of yeast [Microbial cell (Graz, Austria) · 2017Article
- De novo [PSIScientific reports · 2017Article
- Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport.PLoS genetics · 2016Article
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3 authors at 1 institution in 1 country.
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Abstract
Prions are self-propagating, infectious proteins that underlie several neurodegenerative diseases. The molecular basis underlying their sporadic formation is poorly understood. We show that autophagy protects against de novo formation of [PSI(+)], which is the prion form of the yeast Sup35 translation termination factor. Autophagy is a cellular degradation system, and preventing autophagy by mutating its core components elevates the frequency of spontaneous [PSI(+)] formation. Conversely, increasing autophagic flux by treating cells with the polyamine spermidine suppresses prion formation in mutants that normally show a high frequency of de novo prion formation. Autophagy also protects against the de novo formation of another prion, namely the Rnq1/[PIN(+)] prion, which is not related in sequence to the Sup35/[PSI(+)] prion. We show that growth under anaerobic conditions in the absence of molecular oxygen abrogates Sup35 protein damage and suppresses the high frequency of [PSI(+)] formation in an autophagy mutant. Autophagy therefore normally functions to remove oxidatively damaged Sup35, which accumulates in cells grown under aerobic conditions, but in the absence of autophagy, damaged/misfolded Sup35 undergoes structural transitions favoring its conversion to the propagatable [PSI(+)] form.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.