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Titolo:
Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: evidence for direct interaction with the export receptor CRM1
Autore:
Rosorius, O; Reichart, B; Kratzer, F; Heger, P; Dabauvalle, MC; Hauber, J;
Indirizzi:
Univ Erlangen Nurnberg, Inst Clin & Mol Virol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany Univ Wurzburg, Theodor Boveri Inst, Dept Cell & Dev Biol, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 v Biol, D-97074 Wurzburg, Germany
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 14, volume: 112, anno: 1999,
pagine: 2369 - 2380
SICI:
0021-9533(199907)112:14<2369:NPLANT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYPUSINE-CONTAINING PROTEIN; VIRUS TYPE-1 REV; EUKARYOTIC INITIATION FACTOR-5A; MESSENGER-RNA EXPORT; COMPLEX PROTEIN; POSTTRANSLATIONAL FORMATION; INTRANUCLEAR FILAMENTS; MONOCLONAL-ANTIBODIES; HIV-1 REPLICATION; ACTIVATION DOMAIN;
Keywords:
eIF-5A; CRM1; nuclear pore complex; nuclear export; HIV-1; Rev;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
86
Recensione:
Indirizzi per estratti:
Indirizzo: Hauber, J Univ Erlangen Nurnberg, Inst Clin & Mol Virol, Schlossgarten 4, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Schlossgarten 4 Erlangen Germany D-91054
Citazione:
O. Rosorius et al., "Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: evidence for direct interaction with the export receptor CRM1", J CELL SCI, 112(14), 1999, pp. 2369-2380

Abstract

Eukaryotic initiation factor 5A (eIF-5A) is the only cellular protein known to contain the unusual amino acid hypusine. The exact in vivo function ofeIF-5A, however, is to date unknown. The finding that eIF-5A is an essential cofactor of the human immunodeficiency virus type 1 (HIV-1) Rev RNA transport factor suggested that eIF-5A is part of a specific nuclear export pathway. In this study we used indirect immunofluorescence and immunogold electron microscopy to demonstrate that eIF-5A accumulates at nuclear pore-associated intranuclear filaments in mammalian cells and Xenopus oocytes, We are able to show that eIF-5A interacts with the general nuclear export receptor, CRM1. Furthermore, microinjection studies in somatic cells revealed that eIF-5A is transported from the nucleus to the cytoplasm, and that this nuclear export is blocked by leptomycin B. Our data demonstrate that eIF-5A is a nucleocytoplasmic shuttle protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 03:55:22