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- W4377291337 startingPage "e1010774" @default.
- W4377291337 abstract "Pbp1 (poly(A)-binding protein—binding protein 1) is a cytoplasmic stress granule marker that is capable of forming condensates that function in the negative regulation of TORC1 signaling under respiratory conditions. Polyglutamine expansions in its mammalian ortholog ataxin-2 lead to spinocerebellar dysfunction due to toxic protein aggregation. Here, we show that loss of Pbp1 in S . cerevisiae leads to decreased amounts of mRNAs and mitochondrial proteins which are targets of Puf3, a member of the PUF (Pumilio and FBF) family of RNA-binding proteins. We found that Pbp1 supports the translation of Puf3-target mRNAs in respiratory conditions, such as those involved in the assembly of cytochrome c oxidase and subunits of mitochondrial ribosomes. We further show that Pbp1 and Puf3 interact through their respective low complexity domains, which is required for Puf3-target mRNA translation. Our findings reveal a key role for Pbp1-containing assemblies in enabling the translation of mRNAs critical for mitochondrial biogenesis and respiration. They may further explain prior associations of Pbp1/ataxin-2 with RNA, stress granule biology, mitochondrial function, and neuronal health." @default.
- W4377291337 created "2023-05-23" @default.
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- W4377291337 date "2023-05-22" @default.
- W4377291337 modified "2023-09-26" @default.
- W4377291337 title "Pbp1 associates with Puf3 and promotes translation of its target mRNAs involved in mitochondrial biogenesis" @default.
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- W4377291337 doi "https://doi.org/10.1371/journal.pgen.1010774" @default.
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