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Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.

Molecular and cellular biology - 1 Jan 2006

Ganusova Elena E, Ozolins Laura N, Bhagat Srishti, Newnam Gary P, Wegrzyn Renee D, Sherman Michael Y, Chernoff Yury O

Abstract excerpt

Self-perpetuating protein aggregates transmit prion diseases in mammals and heritable traits in yeast. De novo prion formation can be induced by transient overproduction of the corresponding prion-forming protein or its prion domain. Here, we demonstrate that the yeast prion protein Sup35 interacts with various proteins of the actin cortical cytoskeleton that are involved in endocytosis. Sup35-derived aggregates,...

Topics

Actins
Carrier Proteins
Cytoskeletal Proteins
Cytoskeleton
Endocytosis
Mutation
Peptide Termination Factors
Prions
Protein Binding
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

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PMID: 16382152
DOI: 10.1128/MCB.26.2.617-629.2006
PMCID: PMC1346895

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