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• W2157253966 abstract "In metazoans, nuclear export of bulk mRNA is mediated by Tap-p15, a conserved heterodimeric export receptor that cooperates with adaptor RNA-binding proteins. In this article, we show that Thoc5, a subunit of the mammalian TREX complex, binds to a distinct surface on the middle (Ntf2-like) domain of Tap. Notably, adaptor protein Aly and Thoc5 can simultaneously bind to non-overlapping binding sites on Tap-p15. In vivo, Thoc5 was not required for bulk mRNA export. However, nuclear export of HSP70 mRNA depends on both Thoc5 and Aly. Consistent with a function as a specific export adaptor, Thoc5 exhibits in vitro RNA-binding activity and is associated with HSP70 mRNPs in vivo as a component of the stable THO complex. Thus, through the combinatorial use of an adaptor (e.g., Aly) and co-adapter (e.g., Thoc5), Tap-p15 could function as an export receptor for different classes of mRNAs." @default.
• W2157253966 created "2016-06-24" @default.
• W2157253966 creator A5057468179 @default.
• W2157253966 creator A5084921992 @default.
• W2157253966 creator A5085286787 @default.
• W2157253966 creator A5088207071 @default.
• W2157253966 date "2009-01-22" @default.
• W2157253966 modified "2023-10-13" @default.
• W2157253966 title "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA" @default.
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• W2157253966 doi "https://doi.org/10.1038/emboj.2009.5" @default.
• W2157253966 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2657587" @default.
• W2157253966 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19165146" @default.
• W2157253966 hasPublicationYear "2009" @default.
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