Evidence map›Paper›PMID 30301920›Full record

ArticleScientific reports2018

Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF.

Richard B Tunnicliffe, Xiaochen Tian, Joanna Storer, Rozanne M Sandri-Goldin, Alexander P Golovanov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  2. Article
  3. Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Richard B TunnicliffeManchester Institute of Biotechnology, School of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, M1 7DN, UK.
Xiaochen TianDepartment of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, CA, 92697-4025, USA.
Joanna StorerManchester Institute of Biotechnology, School of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, M1 7DN, UK.
Rozanne M Sandri-GoldinDepartment of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, CA, 92697-4025, USA. rmsandri@uci.edu.ORCID http://orcid.org/0000-0003-1825-9830
Alexander P GolovanovManchester Institute of Biotechnology, School of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, M1 7DN, UK. a.golovanov@manchester.ac.uk.ORCID http://orcid.org/0000-0002-8592-3984
University of Manchester · GBUniversity of California, Irvine · US

Funding

Role of cooperative interactions of HSV multifunctional protein ICP27R01AI107803 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI GOLOVANOV, ALEXANDER P., SANDRI-GOLDIN, ROZANNE M · 2013 to 2017
$1.6M
NIAID NIH HHS R01 AI107803
6 · The paper itself

Abstract

The TREX complex mediates the passage of bulk cellular mRNA export to the nuclear export factor TAP/NXF1 via the export adaptors ALYREF or UIF, which appear to act in a redundant manner. TREX complex recruitment to nascent RNA is coupled with 5' capping, splicing and polyadenylation. Therefore to facilitate expression from their intronless genes, herpes viruses have evolved a mechanism to circumvent these cellular controls. Central to this process is a protein from the conserved ICP27 family, which binds viral transcripts and cellular TREX complex components including ALYREF. Here we have identified a novel interaction between HSV-1 ICP27 and an N-terminal domain of UIF in vivo, and used NMR spectroscopy to locate the UIF binding site within an intrinsically disordered region of ICP27. We also characterized the interaction sites of the ICP27 homolog ORF57 from KSHV with UIF and ALYREF using NMR, revealing previously unidentified binding motifs. In both ORF57 and ICP27 the interaction sites for ALYREF and UIF partially overlap, suggestive of mutually exclusive binding. The data provide a map of the binding sites responsible for promoting herpes virus mRNA export, enabling future studies to accurately probe these interactions and reveal the functional consequences for UIF and ALYREF redundancy.

Indexed as

Active Transport, Cell NucleusBinding SitesCell NucleusExodeoxyribonucleasesGene Expression Regulation, ViralHerpesvirus 1, HumanHerpesvirus 8, HumanHost-Pathogen InteractionsHumansImmediate-Early ProteinsIntronsNuclear Magnetic Resonance, BiomolecularNuclear ProteinsNucleocytoplasmic Transport ProteinsPhosphoproteinsProtein BindingALYREF protein, humanExodeoxyribonucleasesICP27 protein, human herpesvirus 1Immediate-Early ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, humanORF57 protein, human herpesvirus 8PhosphoproteinsRNA-Binding ProteinsRNA, Messengerthree prime repair exonuclease 1Transcription FactorsViral Regulatory and Accessory Proteins

Identifiers

PMID30301920
PMCPMC6177440
OpenAlexW2894577325

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.