Evidence map›Paper›PMID 21512126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Coactivators necessary for transcriptional output of the hypoxia inducible factor, HIF, are directly recruited by ARNT PAS-B.

Carrie L Partch, Kevin H Gardner

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 68 citations in OpenAlex.

  1. Context-dependent variability of HIF heterodimers influences interactions with macromolecular and small molecule partners.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  19. Assembly and function of bHLH-PAS complexes.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Formation of a repressive complex in the mammalian circadian clock is mediated by the secondary pocket of CRY1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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

2 authors at 1 institution in 1 country.

Carrie L PartchDepartment of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-8816, USA.
Kevin H Gardner
The University of Texas Southwestern Medical Center · US

Funding

Structural studies of PAS domain signaling mechanismsR01GM081875 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2007 to 2010
$1.2M
Molecular basis of selectivity for coactivator recruitment by ARNT PAS domainsF32CA130441 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI PARTCH, CARRIE L · 2007 to 2009
$148k
NCI NIH HHS CA130441NCI NIH HHS F32 CA130441NIGMS NIH HHS GM081875NIGMS NIH HHS R01 GM081875
6 · The paper itself

Abstract

Hypoxia-inducible factor (HIF) is the key transcriptional effector of the hypoxia response in eukaryotes, coordinating the expression of genes involved in oxygen transport, glycolysis, and angiogenesis to promote adaptation to low oxygen levels. HIF is a basic helix-loop-helix (bHLH)-PAS (PER-ARNT-SIM) heterodimer composed of an oxygen-labile HIF-α subunit and a constitutively expressed aryl hydrocarbon receptor nuclear translocator (ARNT) subunit, which dimerize via basic helix-loop-helix and PAS domains, and recruit coactivators via HIF-α C-terminal transactivation domains. Here we demonstrate that the ARNT PAS-B domain provides an additional recruitment site by binding the coactivator transforming acidic coiled-coil 3 (TACC3) in a step necessary for transcriptional responses to hypoxia. Structural insights from NMR spectroscopy illustrate how this PAS domain simultaneously mediates interactions with HIF-α and TACC3. Finally, mutations on ARNT PAS-B modulate coactivator selectivity and target gene induction by HIF in vivo, demonstrating a bifunctional role for transcriptional regulation by PAS domains within bHLH-PAS transcription factors.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAryl Hydrocarbon Receptor Nuclear TranslocatorBasic Helix-Loop-Helix ProteinsEndothelial PAS Domain-Containing Protein 1HEK293 CellsHumansHypoxia-Inducible Factor 1, alpha SubunitMicrotubule-Associated ProteinsModels, MolecularMolecular Sequence DataMultiprotein ComplexesMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsRecombinant ProteinsARNT protein, humanAryl Hydrocarbon Receptor Nuclear TranslocatorBasic Helix-Loop-Helix ProteinsEndothelial PAS Domain-Containing Protein 1HIF1A protein, humanHypoxia-Inducible Factor 1, alpha SubunitMicrotubule-Associated ProteinsMultiprotein ComplexesRecombinant ProteinsRNA, MessengerTACC3 protein, human

Identifiers

PMID21512126
PMCPMC3093465
OpenAlexW2117186539

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.