Evidence map›Paper›PMID 31641093›Full record

ArticlemBio2019

Molecular Mechanism of SR Protein Kinase 1 Inhibition by the Herpes Virus Protein ICP27.

Richard B Tunnicliffe, William K Hu, Michele Y Wu, Colin Levy, A Paul Mould, Edward A McKenzie, Rozanne M Sandri-Goldin, Alexander P Golovanov

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
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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

8 authors at 2 institutions in 2 countries.

Richard B TunnicliffeManchester Institute of Biotechnology and Department of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, United Kingdom.
William K HuDepartment of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, California, USA.
Michele Y WuDepartment of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, California, USA.
Colin LevyManchester Institute of Biotechnology and Department of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, United Kingdom.
A Paul MouldBiomolecular Analysis Core Facility, Faculty of Biology, Medicine and Health, University of Manchester, United Kingdom.
Edward A McKenzieManchester Institute of Biotechnology and Department of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, United Kingdom.
Rozanne M Sandri-GoldinDepartment of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, California, USA rmsandri@uci.edu a.golovanov@manchester.ac.uk.
Alexander P GolovanovManchester Institute of Biotechnology and Department of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, United Kingdom rmsandri@uci.edu a.golovanov@manchester.ac.uk.
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

Serine-arginine (SR) protein kinase 1 (SRPK1) catalyzes the phosphorylation of SR proteins, which are a conserved family of splicing factors that contain a domain rich in arginine and serine repeats. SR proteins play important roles in constitutive pre-mRNA splicing and are also important regulators of alternative splicing. During herpes simplex virus infection, SRPK1 is inactivated and its cellular distribution is markedly altered by interaction with the viral protein ICP27, resulting in hypophosphorylation of SR proteins. Mutational analysis previously showed that the RGG box motif of ICP27 is required for interaction with SRPK1; however, the mechanism for the inhibition and the exact role of the RGG box was unknown. Here, we used solution nuclear magnetic resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC) to demonstrate that the isolated peptide comprising the RGG box of ICP27 binds to SRPK1 with high affinity, competing with a native substrate, the SR repeat region of SR protein SRSF1. We determined the crystal structure of the complex between SRPK1 and an RGG box peptide, which revealed that the viral peptide binds to the substrate docking groove, mimicking the interactions of SR repeats. Site-directed mutagenesis within the RGG box further confirmed the importance of selected arginine residues for interaction, relocalization, and inhibition of SRPK1

Indexed as

Alternative SplicingCalorimetryHumansImmediate-Early ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesRNA SplicingVirus ReplicationICP27 protein, human herpesvirus 1Immediate-Early ProteinsProtein Serine-Threonine KinasesSRPK1 protein, humanherpes simplex virusphosphorylationsplicingSR protein kinasestructure

Identifiers

PMID31641093
PMCPMC6805999
OpenAlexW2982064449

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.