eEF1A Mediates the Nuclear Export of SNAG-Containing Proteins via the Exportin5-Aminoacyl-tRNA Complex
Author(s) -
José Manuel Mingot,
Sonia Vega,
Amparo Cano,
Francisco Portillo,
M. Ángela Nieto
Publication year - 2013
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2013.09.030
Subject(s) - nuclear export signal , transcription factor , microbiology and biotechnology , biology , transcription (linguistics) , aminoacyl trna , nuclear transport , eukaryotic translation elongation factor 1 alpha 1 , phosphorylation , cytoplasm , elongation factor , transfer rna , rna , cell nucleus , gene , genetics , ribosome , linguistics , philosophy
Exportin5 mediates the nuclear export of double-stranded RNAs, including pre-microRNAs, adenoviral RNAs, and tRNAs. When tRNAs are aminoacylated, the Exportin5-aminoacyl (aa)-tRNA complex recruits and coexports the translation elongation factor eEF1A. Here, we show that eEF1A binds to Snail transcription factors when bound to their main target, the E-cadherin promoter, facilitating their export to the cytoplasm in association with the aa-tRNA-Exportin5 complex. Snail binds to eEF1A through the SNAG domain, a protein nuclear export signal present in several transcription factor families, and this binding is regulated by phosphorylation. Thus, we describe a nuclear role for eEF1A and provide a mechanism for protein nuclear export that attenuates the activity of SNAG-containing transcription factors.
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