Evidence map›Paper›PMID 17565989›Full record

ArticleThe Journal of biological chemistry2007

PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element.

Kenta Iwasaki, Kiros Hailemariam, Yoshiaki Tsuji

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. A novel view of ferritin in cancer.Biochimica et biophysica acta. Reviews on cancer · 2023
    Review
  3. Review
  4. Down-regulation of ATF1 leads to early neuroectoderm differentiation of human embryonic stem cells by increasing the expression level of SOX2.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  5. Article
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  10. Synchrotron radiation induced X-ray emission studies of the antioxidant mechanism of the organoselenium drug ebselen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
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  17. 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

3 authors at 1 institution in 1 country.

Kenta IwasakiDepartment of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, North Carolina 27695, USA.
Kiros Hailemariam
Yoshiaki Tsuji
North Carolina State University · US

Funding

TRAINING IN BIOCHEMICAL AND ENVIRONMENTAL TOXICOLOGYT32ES007046 · NIEHS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI Seth William Kullman · 1985 to 2026
$5.1M
REGULATION OF IRON HOMEOSTASIS IN OXIDATIVE STRESSR01DK060007 · NIDDK · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI TSUJI, YOSHIAKI · 2002 to 2005
$1.2M
NIDDK NIH HHS DK-60007NIDDK NIH HHS DK-60007SNIDDK NIH HHS R01 DK060007NIEHS NIH HHS ES-007046
6 · The paper itself

Abstract

Gene transcription is coordinately regulated by the balance between activation and repression mechanisms in response to various external stimuli. Ferritin, composed of H and L subunits, is the major intracellular iron storage protein involved in iron homeostasis. We previously identified an enhancer, termed antioxidant-responsive element (ARE), in the human ferritin H gene and its respective transcriptional activators including Nrf2 and JunD. Here we found that ATF1 (activating transcription factor 1) is a transcriptional repressor of the ferritin H ARE. Subsequent yeast two-hybrid screening identified PIAS3 (protein inhibitor of activated STAT3) as an ATF1-binding protein. Further investigation of the human ferritin H ARE regulation showed that 1) PIAS3 reversed ATF1-mediated repression of the ferritin H ARE; 2) ATF1 was sumoylated, but PIAS3, a SUMO E3 ligase, did not appear to play a major role in SUMO1-mediated ATF1 sumoylation or ATF1 transcription activating function; 3) PIAS3 decreased ATF1 binding to the ARE; and 4) ATF1 knockdown with siRNA increased ferritin H expression, whereas PIAS3 knockdown decreased basal expression and oxidative stress-mediated induction of ferritin H. These results suggest that PIAS3 antagonizes the repressor function of ATF1, at least in part by blocking its DNA binding, and ultimately activates the ARE. Collectively our results suggest that PIAS3 is a new regulator of ATF1 that regulates the ARE-mediated transcription of the ferritin H gene.

Indexed as

Activating Transcription Factor 1AnimalsAntioxidantsApoferritinsDNA-Binding ProteinsHumansK562 CellsMiceMolecular ChaperonesNF-E2-Related Factor 2NIH 3T3 CellsNuclear ProteinsProtein BindingProtein Inhibitors of Activated STATRegulatory Factor X Transcription FactorsRNA, Small InterferingActivating Transcription Factor 1AntioxidantsApoferritinsATF1 protein, humanAtf1 protein, mouseDNA-Binding ProteinsMolecular ChaperonesNF-E2-Related Factor 2Nuclear ProteinsPIAS3 protein, humanPias3 protein, mouseProtein Inhibitors of Activated STATRegulatory Factor X Transcription FactorsRNA, Small InterferingSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanTranscription Factors

Identifiers

PMID17565989
PMCPMC2409283
OpenAlexW2021980585

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.