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Actin impacts the late stages of prion formation and prion propagation

https://doi.org/10.1101/145060
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb00675.xopenalex-snapshot
Propagation of the yeast prion‐like [psi+] determinant is mediated by oligomerization of the SUP35‐encoded polypeptide chain release factor.
inferredcites →https://doi.org/10.1002/yea.1341openalex-snapshot
An engineered nonsense URA3 allele provides a versatile system to detect the presence, absence and appearance of the [PSI+] prion in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1002/yea.1740openalex-snapshot
Most, but not all, yeast strains in the deletion library contain the [PIN+] prion
inferredcites →https://doi.org/10.1007/bf00341717openalex-snapshot
Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast
inferredcites →https://doi.org/10.1007/bf00351802openalex-snapshot
Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1007/s002840010251openalex-snapshot
Guanidine Hydrochloride Inhibits Hsp104 Activity In Vivo: A Possible Explanation for Its Effect in Curing Yeast Prions
inferredcites →https://doi.org/10.1007/s00438-002-0726-xopenalex-snapshot
Identification of a role for actin in translational fidelity in yeast
inferredcites →https://doi.org/10.1016/j.cell.2014.09.026openalex-snapshot
Organelle-Based Aggregation and Retention of Damaged Proteins in Asymmetrically Dividing Cells
inferredcites →https://doi.org/10.1016/j.celrep.2015.04.060openalex-snapshot
The CPEB3 Protein Is a Functional Prion that Interacts with the Actin Cytoskeleton
inferredcites →https://doi.org/10.1016/j.cub.2017.01.069openalex-snapshot
Compartmentalization of ER-Bound Chaperone Confines Protein Deposit Formation to the Aging Yeast Cell
inferredcites →https://doi.org/10.1016/j.molcel.2011.07.001openalex-snapshot
Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton
inferredcites →https://doi.org/10.1016/s0092-8674(01)00427-5openalex-snapshot
Prions Affect the Appearance of Other Prions
inferredcites →https://doi.org/10.1016/s0092-8674(01)00440-8openalex-snapshot
Multiple Gln/Asn-Rich Prion Domains Confer Susceptibility to Induction of the Yeast [PSI] Prion
inferredcites →https://doi.org/10.1016/s0960-9822(00)00859-9openalex-snapshot
Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton
inferredcites →https://doi.org/10.1016/s1097-2765(00)80412-8openalex-snapshot
Rnq1
inferredcites →https://doi.org/10.1021/bi962388+openalex-snapshot
Mutational Analysis of the Role of the N Terminus of Actin in Actomyosin Interactions. Comparison with Other Mutant Actins and Implications for the Cross-Bridge Cycle
inferredcites →https://doi.org/10.1038/ncomms11265openalex-snapshot
Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast
inferredcites →https://doi.org/10.1038/nrm2818openalex-snapshot
Emerging role for the cytoskeleton as an organizer and regulator of translation
inferredcites →https://doi.org/10.1038/nsb0195-28openalex-snapshot
Defining protein interactions with yeast actin in vivo
inferredcites →https://doi.org/10.1038/s41598-017-00135-6openalex-snapshot
De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers
inferredcites →https://doi.org/10.1038/sj.onc.1201487openalex-snapshot
Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02224.xopenalex-snapshot
The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion‐like elements [PSI + ] and [PIN + ]
inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02478.xopenalex-snapshot
The elimination of the yeast [ PSI + ] prion by guanidine hydrochloride is the result of Hsp104 inactivation
inferredcites →https://doi.org/10.1073/pnas.022462899openalex-snapshot
Actin cable dynamics in budding yeast
inferredcites →https://doi.org/10.1073/pnas.0404968101openalex-snapshot
Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [ PSI + ] prion in yeast and aggregation of Sup35 in vitro
inferredcites →https://doi.org/10.1073/pnas.0808934105openalex-snapshot
Specificity of the J-protein Sis1 in the propagation of 3 yeast prions
inferredcites →https://doi.org/10.1073/pnas.1000347107openalex-snapshot
Ribosome-associated peroxiredoxins suppress oxidative stress–induced de novo formation of the [ PSI + ] prion in yeast
inferredcites →https://doi.org/10.1073/pnas.1132162100openalex-snapshot
Vam10p defines a Sec18p-independent step of priming that allows yeast vacuole tethering
inferredcites →https://doi.org/10.1073/pnas.152330699openalex-snapshot
Interactions among prions and prion “strains” in yeast
inferredcites →https://doi.org/10.1073/pnas.161215198openalex-snapshot
The yeast mutant vps5 Δ affected in the recycling of Golgi membrane proteins displays an enhanced vacuolar Mg 2+ /H + exchange activity
inferredcites →https://doi.org/10.1073/pnas.97.1.240openalex-snapshot
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [ PSI + ] of Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1074/jbc.m609597200openalex-snapshot
Effects of Ubiquitin System Alterations on the Formation and Loss of a Yeast Prion
inferredcites →https://doi.org/10.1074/jbc.r110.113795openalex-snapshot
eEF1A: Thinking Outside the Ribosome
inferredcites →https://doi.org/10.1083/jcb.126.2.413openalex-snapshot
Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin.
inferredcites →https://doi.org/10.1083/jcb.126.2.423openalex-snapshot
Mapping actin surfaces required for functional interactions in vivo.
inferredcites →https://doi.org/10.1083/jcb.98.3.934openalex-snapshot
Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae.
inferredcites →https://doi.org/10.1091/mbc.01-10-0512openalex-snapshot
Genomic Analysis of Homotypic Vacuole Fusion
inferredcites →https://doi.org/10.1091/mbc.4.12.1277openalex-snapshot
Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site.
inferredcites →https://doi.org/10.1091/mbc.9.12.3259openalex-snapshot
Three-dimensional Imaging of the Yeast Actin Cytoskeleton through the Budding Cell Cycle
inferredcites →https://doi.org/10.1093/emboj/19.9.1942openalex-snapshot
Dependence and independence of [PSI+] and [PIN+]: a two‐prion system in yeast?
inferredcites →https://doi.org/10.1093/genetics/132.2.337openalex-snapshot
Systematic mutational analysis of the yeast ACT1 gene.
inferredcites →https://doi.org/10.1093/genetics/144.4.1375openalex-snapshot
Genesis and Variability of [PSI] Prion Factors in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1093/genetics/147.2.507openalex-snapshot
Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1093/genetics/153.1.81openalex-snapshot
Genetic Study of Interactions Between the Cytoskeletal Assembly Protein Sla1 and Prion-Forming Domain of the Release Factor Sup35 (eRF3) in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1093/genetics/157.2.533openalex-snapshot
Generation of an Isogenic Collection of Yeast Actin Mutants and Identification of Three Interrelated Phenotypes
inferredcites →https://doi.org/10.1093/genetics/98.4.691openalex-snapshot
AGENTS THAT CAUSE A HIGH FREQUENCY OF GENETIC CHANGE FROM [psi +] TO [psi -] IN SACCHAROMYCES CEREVISIAE
inferredcites →https://doi.org/10.1101/gad.439307openalex-snapshot
Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
inferredcites →https://doi.org/10.1126/science.1098007openalex-snapshot
Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers
inferredcites →https://doi.org/10.1126/science.1197785openalex-snapshot
A Size Threshold Limits Prion Transmission and Establishes Phenotypic Diversity
inferredcites →https://doi.org/10.1126/science.7754373openalex-snapshot
Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ psi + ]
inferredcites →https://doi.org/10.1126/science.7909170openalex-snapshot
[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/mcb.00201-09openalex-snapshot
The Yeast AAA+ Chaperone Hsp104 Is Part of a Network That Links the Actin Cytoskeleton with the Inheritance of Damaged Proteins
inferredcites →https://doi.org/10.1128/mcb.21.14.4656-4669.2001openalex-snapshot
Mechanism of Prion Loss after Hsp104 Inactivation in Yeast
inferredcites →https://doi.org/10.1128/mcb.22.15.5593-5605.2002openalex-snapshot
Guanidine Hydrochloride Inhibits the Generation of Prion “Seeds” but Not Prion Protein Aggregation in Yeast
inferredcites →https://doi.org/10.1128/mcb.26.2.617-629.2006openalex-snapshot
Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast
inferredcites →https://doi.org/10.1128/mmbr.00013-06openalex-snapshot
The Yeast Actin Cytoskeleton: from Cellular Function to Biochemical Mechanism
inferredcites →https://doi.org/10.1146/annurev.cellbio.19.111401.093127openalex-snapshot
Actin Assembly and Endocytosis: From Yeast to Mammals
inferredcites →https://doi.org/10.1242/jcs.065698openalex-snapshot
Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo
inferredcites →https://doi.org/10.1242/jcs.112.9.1325openalex-snapshot
New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites
inferredcites →https://doi.org/10.1371/journal.pbio.0050024openalex-snapshot
Hsp104-Dependent Remodeling of Prion Complexes Mediates Protein-Only Inheritance
inferredcites →https://doi.org/10.1371/journal.pbio.0060294openalex-snapshot
Prion Switching in Response to Environmental Stress
inferredcites →https://doi.org/10.1371/journal.pgen.1001386openalex-snapshot
Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes
inferredcites →https://doi.org/10.1371/journal.pgen.1004539openalex-snapshot
Essential Genetic Interactors of SIR2 Required for Spatial Sequestration and Asymmetrical Inheritance of Protein Aggregates
inferredcites →https://doi.org/10.1371/journal.pgen.1004814openalex-snapshot
Heterologous Aggregates Promote De Novo Prion Appearance via More than One Mechanism
inferredcites →https://doi.org/10.1371/journal.pgen.1006324openalex-snapshot
Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport
inferredcites →https://doi.org/10.1534/genetics.109.110213openalex-snapshot
The Spontaneous Appearance Rate of the Yeast Prion [PSI+] and Its Implications for the Evolution of the Evolvability Properties of the [PSI+] System
inferredcites →https://doi.org/10.1534/genetics.110.114942openalex-snapshot
Correction/Completion of the Yeast Actin, Alanine Scan Alleles
inferredcites →https://doi.org/10.1534/genetics.111.137760openalex-snapshot
Prions in Yeast
inferredcites →https://doi.org/10.1534/genetics.112.145540openalex-snapshot
Actin and Endocytosis in Budding Yeast
inferredcites →https://doi.org/10.3727/000000001783992650openalex-snapshot
An Antiprion Effect of the Anticytoskeletal Drug Latrunculin A in Yeast
inferredcites →https://doi.org/10.4161/pri.1.3.4840openalex-snapshot
Prion and Nonprion Amyloids
inferredcites →https://doi.org/10.7554/elife.06197openalex-snapshot
Protein aggregates are associated with replicative aging without compromising protein quality control
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