Evidence map›Paper›PMID 23012367›Full record

ArticleThe Journal of biological chemistry2012

Sumoylation is important for stability, subcellular localization, and transcriptional activity of SALL4, an essential stem cell transcription factor.

Feikun Yang, Yixin Yao, Yongping Jiang, Luo Lu, Yupo Ma, Wei Dai

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Protein sumoylation in normal and cancer stem cells.Frontiers in molecular biosciences · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. SUMOylation in brain ischemia: Patterns, targets, and translational implications.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. SALL4: engine of cell stemness.Current gene therapy · 2014
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Feikun YangDepartment of Environmental Medicine, New York University Langone Medical Center, 57 Old, Forge Road, Tuxedo, New York 10987, USA.
Yixin Yao
Yongping Jiang
Luo Lu
Yupo Ma
Wei Dai
Chinese Academy of Medical Sciences & Peking Union Medical College · CNNYU Langone Health · USState University of New York · USUniversity of California, Los Angeles · US

Funding

RESEARCH IN ENVIRONMENTAL HEALTH SCIENCES (CENTER GRANT)P30ES000260 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZELIKOFF, JUDITH TERRY · 1985 to 2020
$26.1M
Molecular mechanisms underlying chromosomal instability and aneuploidyR01CA090658 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAI, WEI · 2001 to 2012
$2.9M
Mechanisms of arsenic-induced chromosomal instability and carcinogenesisR01ES020591 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAI, WEI · 2012 to 2016
$2.0M
Differential Effects of Corneal Hypoxia on Limbal Stem and Epithelial Cell FatesR01EY022364 · NEI · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI LU, LUO · 2012 to 2016
$1.6M
Plk3 in lung cancerR03ES019929 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI XU, DAZHONG · 2011 to 2012
$160k
NCI NIH HHS CA090658NCI NIH HHS R01 CA090658NEI NIH HHS R01 EY022364NIEHS NIH HHS ES000260NIEHS NIH HHS ES019929NIEHS NIH HHS P30 ES000260NIEHS NIH HHS R01 ES020591NIEHS NIH HHS R03 ES019929
6 · The paper itself

Abstract

SALL4 is a transcription factor that plays a key role in the maintenance and self-renewal of embryonic stem cells and hematopoietic stem cells. Given that little is known about regulation of SALL4, we studied biochemical modifications of SALL4B, a major splicing variant of SALL4, and elucidated their biological function. SALL4B was primarily modified by ubiquitination when it was expressed in both Sf9 and HEK293T cells. A significant fraction of SALL4B was further modified by sumoylation when it was expressed in HEK293T cells. Constitutive SUMO-modification of SALL4B was also detected in Tera-1, a cell line of the teratocarcinoma origin. SALL4B sumoylation was independent of ubiquitination and lysine residues 156, 316, 374, and 401 were essential for sumoylation. Chromatin fraction contained more SUMO-deficient SALL4B. Despite a shorter half-life than the wild-type counterpart, SUMO-deficient SALL4B interacted with OCT4 more efficiently than the wild-type SALL4B. RNAi-mediated silencing of SALL4 expression caused significant down-regulation of both OCT4 and SOX2, which was rescued by ectopic expression of SALL4B but not by SUMO-deficient mutant. Significantly, compared with the wild-type SALL4B, SUMO-deficient mutant exhibited compromised trans-activation or trans-repression activities in reporter gene assays. Combined, our studies reveal sumoylation as a novel form of post-translational modification for regulating the stability, subcellular localization, and transcriptional activity of SALL4.

Indexed as

Transcription, GeneticAnimalsCell Line, TumorGenes, ReporterHEK293 CellsHeLa CellsHumansJurkat CellsLysineOctamer Transcription Factor-3RNA InterferenceStem CellsSumoylationTranscriptional ActivationTranscription FactorsLysineOctamer Transcription Factor-3POU5F1 protein, humanSALL4 protein, humanTranscription Factors

Identifiers

PMID23012367
PMCPMC3493905
OpenAlexW1977179273

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.