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

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Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. / Bohnsack, Markus T; Regener, Kathrin; Schwappach, Blanche; Saffrich, Rainer; Paraskeva, Efrosyni; Hartmann, Enno; Görlich, Dirk.

in: EMBO J, Jahrgang 21, Nr. 22, 15.11.2002, S. 6205-15.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Bohnsack, MT, Regener, K, Schwappach, B, Saffrich, R, Paraskeva, E, Hartmann, E & Görlich, D 2002, 'Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm', EMBO J, Jg. 21, Nr. 22, S. 6205-15. https://doi.org/10.1093/emboj/cdf613

APA

Bohnsack, M. T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E., & Görlich, D. (2002). Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J, 21(22), 6205-15. https://doi.org/10.1093/emboj/cdf613

Vancouver

Bohnsack MT, Regener K, Schwappach B, Saffrich R, Paraskeva E, Hartmann E et al. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 2002 Nov 15;21(22):6205-15. https://doi.org/10.1093/emboj/cdf613

Bibtex

@article{14dbcaa1753f4349a433ba51a7291a29,
title = "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm",
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.",
keywords = "3T3 Cells, Active Transport, Cell Nucleus/physiology, Animals, Cell Nucleus/metabolism, Cells, Cultured, Cloning, Molecular, Cricetinae, Cytoplasm/metabolism, Drosophila Proteins/genetics, Drosophila melanogaster/cytology, Eukaryotic Initiation Factors/metabolism, Expressed Sequence Tags, Guanosine Triphosphate/metabolism, HeLa Cells, Humans, Karyopherins/genetics, 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",
author = "Bohnsack, {Markus T} and Kathrin Regener and Blanche Schwappach and Rainer Saffrich and Efrosyni Paraskeva and Enno Hartmann and Dirk G{\"o}rlich",
year = "2002",
month = nov,
day = "15",
doi = "10.1093/emboj/cdf613",
language = "English",
volume = "21",
pages = "6205--15",
journal = "EMBO J",
issn = "0261-4189",
publisher = "NATURE PUBLISHING GROUP",
number = "22",

}

RIS

TY - JOUR

T1 - Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm

AU - Bohnsack, Markus T

AU - Regener, Kathrin

AU - Schwappach, Blanche

AU - Saffrich, Rainer

AU - Paraskeva, Efrosyni

AU - Hartmann, Enno

AU - Görlich, Dirk

PY - 2002/11/15

Y1 - 2002/11/15

N2 - 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.

AB - 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.

KW - 3T3 Cells

KW - Active Transport, Cell Nucleus/physiology

KW - Animals

KW - Cell Nucleus/metabolism

KW - Cells, Cultured

KW - Cloning, Molecular

KW - Cricetinae

KW - Cytoplasm/metabolism

KW - Drosophila Proteins/genetics

KW - Drosophila melanogaster/cytology

KW - Eukaryotic Initiation Factors/metabolism

KW - Expressed Sequence Tags

KW - Guanosine Triphosphate/metabolism

KW - HeLa Cells

KW - Humans

KW - Karyopherins/genetics

KW - Macromolecular Substances

KW - Mesocricetus

KW - Mice

KW - Molecular Sequence Data

KW - Peptide Elongation Factor 1/metabolism

KW - Protein Biosynthesis

KW - Protein Interaction Mapping

KW - Protein Isoforms/metabolism

KW - RNA, Transfer, Amino Acyl/metabolism

KW - Receptors, Cytoplasmic and Nuclear

KW - Recombinant Fusion Proteins/physiology

KW - ran GTP-Binding Protein/metabolism

U2 - 10.1093/emboj/cdf613

DO - 10.1093/emboj/cdf613

M3 - SCORING: Journal article

C2 - 12426392

VL - 21

SP - 6205

EP - 6215

JO - EMBO J

JF - EMBO J

SN - 0261-4189

IS - 22

ER -