Evidence map›Paper›PMID 17267505›Full record

ArticleJournal of virology2007

Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region.

Baode Xie, Cédric F Invernizzi, Stéphane Richard, Mark A Wainberg

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 5% 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

75 citing papers in PubMed, 1 synthesis or guideline pooled it, 129 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The Role of Protein Methyltransferases in Immunity.Molecules (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023
    Review
  13. Review
  14. The Emerging Role of PRMT6 in Cancer.Frontiers in oncology · 2022
    Review
  15. Review
  16. Review
  17. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  18. Article
  19. Article
  20. Review

15 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Baode XieMcGill University AIDS Centre, Department of Medicine, Terry Fox Molecular Oncology Group, Lady Davis Institute, St. Mortimer B. Davis Jewish General Hospital, 3755 Côte-Ste-Catherine Rd., Montréal, Québec H3T 1E2, Canada.
Cédric F Invernizzi
Stéphane Richard
Mark A Wainberg
McGill University · CAJewish General Hospital · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arginine methylation has been shown to regulate signal transduction, protein subcellular localization, gene transcription, and protein-protein interactions that ultimately alter gene expression. Although the role of cellular protein arginine methyltransferases (PRMT) in viral gene expression is largely unknown, we recently showed that the Tat protein of human immunodeficiency virus type 1 (HIV-1) is a substrate for one such enzyme, termed PRMT6. However, the mechanism by which arginine methylation impairs the transactivation potential of Tat and the sites of arginine methylation within Tat remain obscure. We now show that Tat is a specific in vitro and in vivo substrate of PRMT6 which targets the Tat R52 and R53 residues for arginine methylation. Such Tat methylation led to decreased interaction with the Tat transactivation region (TAR) of viral RNA. Furthermore, arginine methylation of Tat negatively affected Tat-TAR-cyclin T1 ternary complex formation and diminished cyclin T1-dependent Tat transcriptional activation. Overexpression of wild-type PRMT6, but not a methylase-inactive PRMT6 mutant, reduced levels of Tat transactivation of HIV-1 long terminal repeat chloramphenicol acetyltransferase and luciferase reporter plasmids in a dose-dependent manner. In cell-based assays, knockdown of PRMT6 resulted in increased HIV-1 production and faster viral replication. Thus, PRMT6 can compromise Tat transcriptional activation and may represent a form of innate cellular immunity in regard to HIV-1 replication. Finding a way of inhibiting or stimulating PRMT6 activity might help to drive quiescently infected cells out of latency or combat HIV-1 replication, respectively.

Indexed as

Transcriptional ActivationArginineCell LineChloramphenicol O-AcetyltransferaseCyclinsCyclin TGene Products, tatGene SilencingGenes, ReporterHIV-1HumansLuciferasesMethylationNuclear ProteinsProtein-Arginine N-MethyltransferasesProtein BindingArginineCCNT1 protein, humanChloramphenicol O-AcetyltransferaseCyclinsCyclin TGene Products, tatLuciferasesNuclear ProteinsPRMT6 protein, humanProtein-Arginine N-MethyltransferasesRNA, Viraltat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID17267505
PMCPMC1866113
OpenAlexW2141815936

What OpenQuestion holds

Textmetadata
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.