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PMID: 12426392 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm.

The EMBO journal ·Vol. 21 ·No. 22 ·2002-11-15 ·Pages 6205-15

Bohnsack MT, Regener K, Schwappach B, Saffrich R, Paraskeva E, Hartmann E, Görlich D

Abstract

Importin beta-type transport receptors mediate the vast majority of transport pathways between cell nucleus and cytoplasm. We identify here the translation elongation factor 1A (eEF1A) as the predominant nuclear export substrate of RanBP21/exportin 5 (Exp5). This cargo-exportin interaction is rather un usual in that eEF1A binds the exportin not directly, but instead via aminoacylated tRNAs. Exp5 thus represents the second directly RNA-binding exportin and mediates tRNA export in parallel with exportin-t. It was suggested recently that 10-15% of the cellular translation would occur in the nucleus. Our data rule out such a scenario and instead suggest that nuclear translation is actively suppressed by the nuclear export machinery. We found that the vast majority of translation initiation factors (eIF2, eIF2B, eIF3, eIF4A1, eIF5 and eIF5B), all three elongation factors (eEF1A, eEF1B and eEF2) and the termination factor eRF1 are strictly excluded from nuclei. Besides Exp5 and importin 13, CRM1 and as yet unidentified exportins also contribute to the depletion of translation factors from nuclei.

MeSH Terms
3T3 Cells Active Transport, Cell Nucleus/physiology Animals Cell Nucleus/metabolism Cells, Cultured Cloning, Molecular Cricetinae Cytoplasm/metabolism Drosophila Proteins/genetics,physiology Drosophila melanogaster/cytology Eukaryotic Initiation Factors/metabolism Expressed Sequence Tags Guanosine Triphosphate/metabolism HeLa Cells Humans Karyopherins/genetics,physiology Macromolecular Substances Mesocricetus Mice Molecular Sequence Data Peptide Elongation Factor 1/metabolism Protein Biosynthesis Protein Interaction Mapping Protein Isoforms/metabolism RNA, Transfer, Amino Acyl/metabolism Receptors, Cytoplasmic and Nuclear Recombinant Fusion Proteins/physiology ran GTP-Binding Protein/metabolism
Chemicals
Drosophila Proteins Eukaryotic Initiation Factors Karyopherins Macromolecular Substances Peptide Elongation Factor 1 Protein Isoforms RNA, Transfer, Amino Acyl RanBP21 protein, Drosophila Receptors, Cytoplasmic and Nuclear Recombinant Fusion Proteins XPO5 protein, human Xpo5 protein, mouse exportin 1 protein Guanosine Triphosphate ran GTP-Binding Protein
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Bohnsack Markus T
ZMBH, INF 282, D-69120 Heidelberg, Germany.
Regener Kathrin
Schwappach Blanche
Saffrich Rainer
Paraskeva Efrosyni
Hartmann Enno
Görlich Dirk
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2002-11-15
Pages
6205-15
Language
English
Region
England
NLM ID
8208664
PMCID
PMC137205
Subset
IM
Databases
GENBANK
AF222746, AF271159, AF343581
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