Evidence map›Paper›PMID 12486002›Full record

ArticleThe EMBO journal2002

Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF.

Vanessa Brès, Hideaki Tagami, Jean-Marie Péloponèse, Erwan Loret, Kuan-Teh Jeang, Yoshihiro Nakatani, Stephane Emiliani, Monsef Benkirane, Rosemary E Kiernan

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
10.9field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  5. Article
  6. Cell death pathways and viruses: Role of microRNAs.Molecular therapy. Nucleic acids · 2021
    Review
  7. Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019
    Review
  8. Review
  9. Review
  10. Functional roles of HIV-1 Tat protein in the nucleus.Cellular and molecular life sciences : CMLS · 2016
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. 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

9 authors at 1 institution in 1 country.

Vanessa BrèsLaboratoire de Virologie Moléculaire et Transfert de Gène, Institut de Génétique Humaine, CNRS UPR1142, Montpellier, France.
Hideaki Tagami
Jean-Marie Péloponèse
Erwan Loret
Kuan-Teh Jeang
Yoshihiro Nakatani
Stephane Emiliani
Monsef Benkirane
Rosemary E Kiernan
Institut de Génétique Humaine · FR

Funding

Molecular Mechanisms Of Human Immunodeficiency Virus Trans-regulatory ProteinsZIAAI000547 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI JEANG, KUAN-TEH · 2009 to 2013
$5.9M
MOLECULAR MECHANISMS OF HUMAN RETROVIRUS TRANS-REGULATORY PROTEINSZ01AI000547 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI JEANG, KUAN-TEH · 1989 to 2008
$2.8M
6 · The paper itself

Abstract

The HIV-1 transactivator protein, Tat, is an atypical transcriptional activator that functions through binding, not to DNA, but to a short leader RNA, TAR. Although details of its functional mechanism are still unknown, emerging findings suggest that Tat serves primarily to adapt co-activator complexes such as p300, PCAF and P-TEFb to the HIV-1 long terminal repeat. Hence, an understanding of how Tat interacts with these cofactors is crucial. It has recently been shown that acetylation at a single lysine, residue 50, regulated the association of Tat with PCAF. Here, we report that in the absence of Tat acetylation, PCAF binds to amino acids 20-40 within Tat. Interestingly, acetylation of Tat at Lys28 abrogates Tat-PCAF interaction. Acetylation at Lys50 creates a new site for binding to PCAF and dictates the formation of a ternary complex of Tat-PCAF-P-TEFb. Thus, differential lysine acetylation of Tat coordinates the interactions with its co-activators, cyclin T1 and PCAF. Our results may help in understanding the ordered recruitment of Tat co-activators to the HIV-1 promoter.

Indexed as

AcetylationAcetyltransferasesBlotting, WesternCell Cycle ProteinsChromatography, AffinityCyclinsCyclin TGene Products, tatGlutathione TransferaseHeLa CellsHistone AcetyltransferasesHIV Long Terminal RepeatHumansLysineModels, BiologicalNuclear ProteinsAcetyltransferasesCCNT1 protein, humanCell Cycle ProteinsCyclinsCyclin TGene Products, tatGlutathione TransferaseHistone AcetyltransferasesLysineNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsPeptidesRecombinant Fusion ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID12486002
PMCPMC139090
OpenAlexW2090040582

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.