Evidence map›Paper›PMID 24728382›Full record

ArticlePloS one2014

Inhibition of Sp1 functions by its sequestration into PML nuclear bodies.

June Li, Wen-Xin Zou, Kun-Sang Chang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Different SP1 binding dynamics at individual genomic loci in human cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Review
  4. Article
  5. [Sensitivity of alternative spliceosomes of L-type PML-RARα fusion gene to ATO].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2017
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

June LiDepartment of Translational Molecular Pathology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas, United States of America.
Wen-Xin ZouDepartment of Translational Molecular Pathology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas, United States of America.
Kun-Sang ChangDepartment of Translational Molecular Pathology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas, United States of America.
The University of Texas MD Anderson Cancer Center · US

Funding

MOLECULAR PATHOLOGY OF ACUTE PROMYELOCYTIC LEUKEMIAR01CA055577 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHANG, KUN-SANG · 1992 to 2012
$2.5M
NCI NIH HHS CA 55577NCI NIH HHS R01 CA055577
6 · The paper itself

Abstract

Promyelocytic leukemia nuclear bodies (PML NBs) are comprised of PML and a striking variety of its associated proteins. Various cellular functions have been attributed to PML NBs, including the regulation of gene expression. We report here that induced expression of PML recruits Sp1 into PML NBs, leading to the reduction of Sp1 transactivation function. Specifically, Chromatin immunoprecipitation (ChIP) assay demonstrated that induced expression of PML significantly diminishes the amount of Sp1 binding to its target gene promoter, immunofluorescence staining showed dramatic increase in the co-localization between PML and Sp1 upon induction of PML expression, moreover, PML and Sp1 co-fractionated in the core nuclear matrix. Our study further showed that PML promotes SUMOylation of Sp1 in a RING-motif-dependent manner, SUMOylation of Sp1 facilitates physical interaction between Sp1 and PML and recruitment of Sp1 into the PML NBs, the SUMO binding motif of PML was also important for its interaction with Sp1. The results of this study demonstrate a novel mechanism by which PML regulates gene expression through sequestration of the transcription factor into PML NBs.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCell LineHumansIntranuclear Inclusion BodiesLeukemia, Promyelocytic, AcuteMiceMolecular Sequence DataNuclear MatrixNuclear ProteinsPromyelocytic Leukemia ProteinProtein BindingProtein Structure, TertiarySp1 Transcription FactorSumoylationNuclear ProteinsPml protein, mousePromyelocytic Leukemia ProteinSp1 Transcription FactorTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID24728382
PMCPMC3984170
OpenAlexW2009040596

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.