Journal
EMBO JOURNAL
Volume 28, Issue 5, Pages 556-567Publisher
WILEY
DOI: 10.1038/emboj.2009.5
Keywords
heat shock mRNA; nucleo-cytoplasmic transport; TREX complex
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Funding
- Japanese Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Takeda Science Foundation
- Human Frontier Science Program
- Grants-in-Aid for Scientific Research [21247032] Funding Source: KAKEN
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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.
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