Interaction of eukaryotic initiation factor 5A (eIF‐5A) with nuclear pore complexes

Reichart, Beate; Rosorius, Olaf; Hauber, Joachim; Dabauvalle, Marie-Christine

doi:10.1016/s0248-4900(98)80260-8

Cited by 3 publications

(2 citation statements)

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“…It can bind specifically to the NES of Rev [135,136]. Non-functional eIF5A mutants that retain the ability to bind Rev hamper the export of Rev-CRM1 complexes to the cytoplasm [135,137]. Indeed, T CD4 lymphocytic cell lines overexpressing these mutants failed to sustain HIV-1 replication efficiently [136].…”

Section: The Rev-host Interactomementioning

confidence: 99%

“…Indeed, T CD4 lymphocytic cell lines overexpressing these mutants failed to sustain HIV-1 replication efficiently [136]. A pool of eIF5A localizes at the periphery of the nuclear pore complex [137] and has been found to interact with nucleoporins [60]. Moreover, recombinant GST-Rev protein export to the cytoplasm was abrogated by using antibodies against eIF5A [138].…”

Section: The Rev-host Interactomementioning

confidence: 99%

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HIV Rev-isited

et al. 2020

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The human immunodeficiency virus type 1 (HIV-1) proteome is expressed from alternatively spliced and unspliced genomic RNAs. However, HIV-1 RNAs that are not fully spliced are perceived by the host machinery as defective and are retained in the nucleus. During late infection, HIV-1 bypasses this regulatory mechanism by expression of the Rev protein from a fully spliced mRNA. Once imported into the nucleus, Rev mediates the export of unprocessed HIV-1 RNAs to the cytoplasm, leading to the production of the viral progeny. While regarded as a canonical RNA export factor, Rev has also been linked to HIV-1 RNA translation, stabilization, splicing and packaging. However, Rev's functions beyond RNA export have remained poorly understood. Here, we revisit this paradigmatic protein, reviewing recent data investigating its structure and function. We conclude by asking: what remains unknown about this enigmatic viral protein?

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Section: The Rev-host Interactomementioning

confidence: 99%

Section: The Rev-host Interactomementioning

confidence: 99%

HIV Rev-isited

et al. 2020

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The adenovirus type 5 E1B-55K oncoprotein is a highly active shuttle protein and shuttling is independent of E4orf6, p53 and Mdm2

et al. 2000

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The E1B-55K and E4orf6 oncoproteins of adenovirus type 5 are involved in the export of viral mRNAs. Previously, it was suggested that a complex composed of E1B-55K and E4orf6 serves as a nucleocytoplasmic transporter for viral mRNAs in which the E4orf6 protein directs both nuclear import and export. We now demonstrate that the E1B-55K protein itself shuttles e ciently in the absence of E4orf6. In addition, E1B-55K tra cking was independent of the de®ned shuttle proteins Mdm2 or p53, which interacts with E1B-55K. The identi®ed N-terminal E1B-55K leucine-rich nuclearexport signal (NES) conferred rapid nuclear export even in a heterologous system in contrast to the postulated E4orf6NES. Interestingly, although shuttling was blocked by inhibitors of the CRM1 mediated export pathway, E1B-55K inhibited neither the activity nor the tra cking of the retroviral shuttle proteins HIV-1 Rev and HTLV-1 Rex. In contrast, Rev or Rex blocked the nuclear export of E1B-55K, most likely by competing for essential export factors. Our results provide new insights into the regulation of the adenovirus mRNA export system and the processes of adenovirus mediated transformation. Oncogene (2000) 19, 850 ± 857.

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Rev Inhibition Strongly Affects Intracellular Distribution of Human Immunodeficiency Virus Type 1 RNAs

Cmarko

Bøe²,

Scassellati

et al. 2002

J Virol

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To define the human immunodeficiency virus type 1 (HIV-1) RNA maturation pathways, we analyzed the intracellular distribution of HIV-1 RNA and the viral regulatory proteins Rev and Tat in transfected COS cells and HIV-1-infected lymphoid C8166 cells by means of ultrastructural in situ hybridization using antisense RNA probes and immunoelectron microscopy. The intranuclear viral RNA occurs in ribonucleoprotein fibrils in the perichromatin and interchromatin regions. The simultaneous demonstration of Rev, Tat, Br-labeled RNA, and cellular proteins SC35 and CRM1 in such fibrils reveals the potential of Rev to associate with nascent HIV pre-mRNA and its splicing complex and transport machinery. In a rev-minus system, the env intron-containing, incompletely spliced viral RNAs are revealed only in the nucleus, indicating that Rev is required to initiate the transport to the cytoplasm. Moreover, env intron sequences frequently occur in the periphery of interchromatin granule clusters, while the probe containing the rev exon sequence does not associate with this nucleoplasmic domain. When cells were treated with the CRM1 inhibitor leptomycin B in the presence of Rev protein, the env intron containing HIV RNAs formed clusters throughout the nucleoplasm and accumulated at the nuclear pores. This suggests that Rev is necessary and probably also sufficient for the accumulation of incompletely spliced HIV RNAs at the nuclear pores while CRM1 is needed for translocation across the nuclear pore complex.During lentivirus replication, the nuclear export of transcribed viral mRNAs from the nucleus to the cytoplasm via the nuclear pore complex is regulated by factors encoded in the viral genome (reviewed in reference 57). The 116-amino-acid Rev protein of human immunodeficiency virus type 1 (HIV-1), a lentivirus, interacts with the viral RNA and mediates its nuclear export. A short arginine-rich domain of Rev binds directly to a 234-nucleotide RNA sequence termed the Rev responsive element (RRE), which is localized in intron RNA (33; for reviews, see references 9 and 40). Completely spliced RNAs appear in the cytoplasm independently of Rev. From these fully spliced RNAs, Rev, together with the transcriptional elongation factor Tat, is translated early in infection. Rev enters the nucleus to induce transport of the intron-containing, Rev-dependent unspliced and partially spliced RNAs, from which the late structural HIV-1 proteins are translated (28,40). In addition to the intron-RNA binding capacity, the basic domain of the Rev protein possesses a nuclear localization sequence. Another domain, a short leucine-rich region located at the carboxy terminus of Rev and called a nuclear export signal (NES), is required for interaction with the cellular export receptors (18,19). Both these domains confer on the Rev protein the possibility of shuttling between the nucleus and the cytoplasm (26,35,52,58). Molecular arrangements and mechanisms by which Rev controls posttranscriptional export of RNA during the viral replication cycle are partl...

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Interaction of eukaryotic initiation factor 5A (eIF‐5A) with nuclear pore complexes

Cited by 3 publications

References 0 publications

HIV Rev-isited

HIV Rev-isited

The adenovirus type 5 E1B-55K oncoprotein is a highly active shuttle protein and shuttling is independent of E4orf6, p53 and Mdm2

Rev Inhibition Strongly Affects Intracellular Distribution of Human Immunodeficiency Virus Type 1 RNAs

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