The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm.

Meyer, Barbara E.; Malim, Michael H.

doi:10.1101/gad.8.13.1538

Cited by 291 publications

(248 citation statements)

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“…Promotion of expression of incompletely ;pliced transcripts in the cytoplasm may involve two activities )f Rex. One, not yet shown directly but inferred from studies m the HIV equivalent Rev [15,16], is that Rex promotes ex~ort of viral RNAs by binding to the RexRE on the RNA md dragging the RNA out of the nucleus. In this respect a ~uclear export signal has been identified on Rex [13].…”

Section: Discussionmentioning

confidence: 99%

Section: ! Introductionmentioning

confidence: 99%

“…A C-terminal domain encodes a leucinerich effector domain which includes a recently characterised nuclear export signal [13,14]. The combination of nuclear import and export signals accounts for the demonstrated ability of Rev to shuttle between the nucleus and cytoplasm [15,16].Two models have been proposed to account for the retention of unspliced viral mRNAs in the nucleus and for the relief of the retention by Rex or Rev. In one the splicing signals of the introns of the larger transcripts of viral RNA are inefficient, and in the absence of Rex or Rev the unspliced RNAs are retained in the nucleus bound 1o spliceosome complexes [17].…”

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confidence: 99%

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Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

White

1996

FEBS Letters

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p27 rex of HTLV-1 promotes nucleocytoplasmic t xport of viral mRNAs through binding of the Rex-response element (RexRE) present at the 3' end of the viral transcripts in ds with respect to the ORFs of the viral mRNAs. We have found that expression of the RexRE in trans, as a separate RNA, still allows Rex protein to promote export of viral mRNAs lacking the RexRE. The data suggest the formation of a ternary complex between Rex protein, RexRE and upstream elements of viral mRNA and hence the existence of secondary sites of interaction between Rex protein and viral RNAs.~ey words: mRNA export; HTLV-1; Retrovirus; p27rex; t,'~ex-responsive element; Fluorescence in situ hybridisation !. IntroductionHuman T-cell leukaemic virus type 1 (HTLV-1) is a retro-, irus trophic for CD4 + T-cells associated with an aggressive lorm of leukaemia, adult T-cell leukaemia [1,2], and with a ~eurological disorder, tropical spastic paraparesis, also due to infection of T-cells [3]. In order to co-ordinate the regulation ,,f the structural and viral proteins necessary for viral replication a nuclear protein, Rex, encoded in the viral genome, makes efficient use of variably spliced reading frames in the , iral genome (reviewed in [4]). In the presence of Rex incom-1,1etely spliced transcripts of viral RNA are expressed in the • ytoplasm, allowing expression of proteins from the unspliced :ag-pol transcript and the singly spliced env transcript. In the ,,bsence of Rex the incompletely spliced transcripts remain .equestered in the nucleus to be degraded or for completion ,,f splicing [5,6]. Completely spliced transcripts encode the ~egulatory proteins of the virus, Tax and Rex [5]. Rex works i~y binding directly to a highly structured element of RNA of ~kbout 250 bases present in the viral transcripts, the Rex-re-, ponsive element (RexRE) [7][8][9]. Details of the mechanism of ~tction of Rex, and its analogue Rev from human immunode-!tciency virus (HIV) type 1, are becoming apparent. Despite ~heir lack of sequence homology both proteins contain two orresponding functional domains. The N-terminal domain is ~ich in basic amino acid residues and serves as a nuclear i ocalisation signal, which also has nucleolar localising capabilty [10]. In addition the same domain is the site for multi-' Corresponding author. Fax: (44) (171) 955-4191. E-mail: k.white@umds.ac.ukIbbreviations. FITC, fluorescein isothiocyanate; HIV, human immunodeficiency virus; HTLV-1, human T-cell leukaemic virus type 1 ; NOS, nucleolar localisation signal; RexRE, Rex-responsive element merisation [11] and for binding to the responsive element on the viral RNA [8,12]. A C-terminal domain encodes a leucinerich effector domain which includes a recently characterised nuclear export signal [13,14]. The combination of nuclear import and export signals accounts for the demonstrated ability of Rev to shuttle between the nucleus and cytoplasm [15,16].Two models have been proposed to account for the retention of unspliced viral mRNAs in the nucleus and for the relief of the ...

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Section: Discussionmentioning

confidence: 99%

Section: ! Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

White

1996

FEBS Letters

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“…The nuclear export signals (NESs) for protein kinase inhibitor (Wen et al, 1995), HIV-1 Rev protein (Fischer et al, 1995), TFIIIA (Fridell et al, 1996), and hnRNP protein Al (Michael et al, 1995) bear no similarity to NLSs (Dingwall and Laskey, 1991). Both the hnRNP Al protein and the Rev protein specifically bind RNA and shuttle back and forth between the nucleus and cytoplasm (Daly et al, 1989;Malim et al, 1989;Zapp and Green, 1989;Pinol-Roma and Dreyfuss, 1992;Meyer and Malim, 1994). Thus, for proteinbound RNA molecules, the mechanism of RNA export may in essence be that of protein export.…”

Section: Introductionmentioning

confidence: 99%

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

Murphy

Watkins

Wente

1996

MBoC

168

164

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To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin NuplOOp were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srplp, the nuclear localization signal receptor, as well as Riplp, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.

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“…The HIV viral protein Rev (regulator of viral expression) is responsible for the nuclear export of unspliced and partially spliced HIV mRNAs (Meyer and Malim, 1994;Pollard and Malim, 1998). To fulfill its role in nuclear export, Rev shuttles between the nucleus and cytoplasm with its NLS and NES.…”

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confidence: 99%

Rev‐GFP transgenic lines for studies of nucleocytoplasmic transport in drosophila

Chan

Tung

O’Kane

2002

Genesis

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The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm.

Cited by 291 publications

References 80 publications

Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

Rev‐GFP transgenic lines for studies of nucleocytoplasmic transport in drosophila

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