Evidence map›Paper›PMID 24843025›Full record

ArticleeLife2014

AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter.

Ursula Schulze-Gahmen, Huasong Lu, Qiang Zhou, Tom Alber

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. 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
2.6field-weighted citation impact, top 10% 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, 55 citations in OpenAlex.

  1. Structural basis for P-TEFb association with BRD4.bioRxiv : the preprint server for biology · 2026
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  18. AFF1 acetylation by p300 temporally inhibits transcription during genotoxic stress response.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 1 institution in 1 country.

Ursula Schulze-GahmenDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States uschulze-gahmen@berkeley.edu.
Huasong LuDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Qiang ZhouDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Tom AlberDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, Berkeley, United States.
University of California, Berkeley · US

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
REGULATION OF TRANSCRIPTIONAL ELONGATION BY HIV1 TATR01AI041757 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZHOU, QIANG · 1997 to 2019
$6.6M
Tat cofactors and control of HIV-1 latencyR01AI095057 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZHOU, QIANG · 2011 to 2015
$1.9M
NIAID NIH HHS R01AI041757NIAID NIH HHS R01 AI095057NIAID NIH HHS R01AI095057NIGMS NIH HHS P50 GM082250NIGMS NIH HHS P50GM82250
6 · The paper itself

Abstract

Superelongation complexes (SECs) are essential for transcription elongation of many human genes, including the integrated HIV-1 genome. At the HIV-1 promoter, the viral Tat protein binds simultaneously to the nascent TAR RNA and the CycT1 subunit of the P-TEFb kinase in a SEC. To understand the preferential recruitment of SECs by Tat and TAR, we determined the crystal structure of a quaternary complex containing Tat, P-TEFb, and the SEC scaffold, AFF4. Tat and AFF4 fold on the surface of CycT1 and interact directly. Interface mutations in the AFF4 homolog AFF1 reduced Tat-AFF1 affinity in vivo and Tat-dependent transcription from the HIV promoter. AFF4 binding in the presence of Tat partially orders the CycT1 Tat-TAR recognition motif and increases the affinity of Tat-P-TEFb for TAR 30-fold. These studies indicate that AFF4 acts as a two-step filter to increase the selectivity of Tat and TAR for SECs over P-TEFb alone.DOI: http://dx.doi.org/10.7554/eLife.02375.001.

Indexed as

Gene Expression Regulation, ViralGene Products, tatGenome, ViralHIV-1HIV Long Terminal RepeatHumansPositive Transcriptional Elongation Factor BPromoter Regions, GeneticProtein BindingProtein ConformationRepressor ProteinsRNA, ViralTranscriptional Elongation FactorsViral ProteinsAFF4 protein, humanGene Products, tatPositive Transcriptional Elongation Factor BRepressor ProteinsRNA, ViralTranscriptional Elongation FactorsViral Proteinscrystal structureTat-AFF4-CycT1 interfaceTat-TAR recognition motiftranscriptional elongation

Identifiers

PMID24843025
PMCPMC4013717
OpenAlexW1968118598

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.