Evidence map›Paper›PMID 19924293›Full record

ArticlePloS one2009

Three distinct domains contribute to nuclear transport of murine Foxp3.

Wayne W Hancock, Engin Ozkaynak

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Inhibition of FOXP3 by stapled alpha-helical peptides dampens regulatory T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. A Structure-Guided Delineation of FOXP3 Regulation Mechanism in IPEX.Advances in experimental medicine and biology · 2021
    Article
  5. FoxP3 in TClinical and experimental immunology · 2020
    Review
  6. Review
  7. FoxP3 scanning mutagenesis reveals functional variegation and mild mutations with atypical autoimmune phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. The regulation of immune tolerance by FOXP3.Nature reviews. Immunology · 2017
    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

2 authors at 1 institution in 1 country.

Wayne W HancockDivision of Transplant Immunology, Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and the University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Engin Ozkaynak
Children's Hospital of Philadelphia · US

Funding

Proteolytic cleavage regulates Foxp3 activityR21AI072420 · NIAID · CHILDREN'S HOSP OF PHILADELPHIA · PI OZKAYNAK, ENGIN · 2009 to 2010
$452k
NIAID NIH HHS 1R21AI72420-01A1NIAID NIH HHS R21 AI072420
6 · The paper itself

Abstract

Foxp3, a 47-kDa transcription factor, is necessary for the function of CD4+CD25+ regulatory T cells (Tregs), with an essential role in the control of self-reactive T cells and in preventing autoimmunity. Activation of Tregs by TCR engagement results in upregulation of Foxp3 expression, followed by its rapid nuclear transport and binding to chromatin. Here, we identify three distinct Foxp3 domains that contribute to nuclear transport. The first domain (Domain 1) comprises the C-terminal 12 amino acids. The second domain (Domain 2) is located immediately N-terminal to the forkhead domain (FHD), recently reported to be a binding site for the runt-related transcription factor 1/acute myeloid leukemia 1 (Runx1/AML1). The third domain (Domain 3) is located within the N-terminal first 51 amino acids. Unlike the known nuclear localization signals (NLSs), none of these three regions are rich in basic residues and do not bear any similarity to known monopartite or bipartite NLSs that have one or more clusters of basic amino acids. The basic arginine-lysine-lysine-arginine (RKKR) sequence, located 12-aa from the C-terminal end of Foxp3 was previously reported to be a nuclear localization signal (NLS) for several proteins, including for a GFP-Foxp3 hybrid. Evidence is provided here that in the full-length native Foxp3 RKKR does not function as an NLS. The data reported in this study indicates that Foxp3 achieves nuclear transport by binding to other nuclear factors and co-transporting with them to the nucleus.

Indexed as

Active Transport, Cell NucleusAmino AcidsAnimalsBinding SitesCell NucleusCloning, MolecularCore Binding Factor Alpha 2 SubunitCytoplasmDNA, ComplementaryFemaleForkhead Transcription FactorsGreen Fluorescent ProteinsMiceMice, Inbred C57BLProtein Structure, TertiaryAmino AcidsCore Binding Factor Alpha 2 SubunitDNA, ComplementaryForkhead Transcription FactorsFoxp3 protein, mouseGreen Fluorescent ProteinsRunx1 protein, mouse

Identifiers

PMID19924293
PMCPMC2774276
OpenAlexW1964948851

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.