Evidence map›Paper›PMID 26212494›Full record

ArticleJournal of cellular biochemistry2016

The Key Regulator for Language and Speech Development, FOXP2, is a Novel Substrate for SUMOylation.

Leslie J Meredith, Chiung-Min Wang, Leticia Nascimento, Runhua Liu, Lizhong Wang, Wei-Hsiung Yang

Abstract read
In one paragraph

Article in Journal of cellular biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Genetic variability ofHeliyon · 2024
    Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
  7. Article
  8. Review
  9. Article
  10. FOXP3 Activates SUMO-ConjugatingInternational journal of molecular sciences · 2018
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016
    Review
  19. Review
  20. Biomarkers in schizophrenia - past, present and future.Romanian journal of morphology and embryology = Revue roumaine de morphologie et embryologie
    Review
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

6 authors at 3 institutions in 1 country.

Leslie J MeredithDepartment of Biomedical Sciences, Mercer University School of Medicine, Savannah, Georgia 30404.
Chiung-Min WangDepartment of Biomedical Sciences, Mercer University School of Medicine, Savannah, Georgia 30404.
Leticia NascimentoDepartment of Biomedical Sciences, Mercer University School of Medicine, Savannah, Georgia 30404.
Runhua LiuDepartment of Genetics and Comprehensive Cancer Center, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Lizhong WangDepartment of Genetics and Comprehensive Cancer Center, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Wei-Hsiung YangDepartment of Biomedical Sciences, Mercer University School of Medicine, Savannah, Georgia 30404.
Mercer University · USMercer University Health Sciences Center · USUniversity of Alabama at Birmingham · US

Funding

MicroRNAs for monitoring tumor progression and predicting response to therapyR21CA179282 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI WANG, LIZHONG · 2014 to 2015
$352k
FOXP3-microRNA146-NFkB Axis in Tumor SuppressionR21CA164688 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI WANG, LIZHONG · 2012 to 2013
$341k
NCI NIH HHS CA164688NCI NIH HHS CA179282NCI NIH HHS R21 CA164688NCI NIH HHS R21 CA179282
6 · The paper itself

Abstract

Transcription factor forkhead box protein P2 (FOXP2) plays an essential role in the development of language and speech. However, the transcriptional activity of FOXP2 regulated by the post-translational modifications remains unknown. Here, we demonstrated that FOXP2 is clearly defined as a SUMO target protein at the cellular levels as FOXP2 is covalently modified by both SUMO1 and SUMO3. Furthermore, SUMOylation of FOXP2 was significantly decreased by SENP2 (a specific SUMOylation protease). We further showed that FOXP2 is selectively SUMOylated in vivo on a phylogenetically conserved lysine 674 but the SUMOylation does not alter subcellular localization and stability of FOXP2. Interestingly, we observed that human etiological FOXP2 R553H mutation robustly reduces its SUMOylation potential as compared to wild-type FOXP2. In addition, the acidic residues downstream the core SUMO motif on FOXP2 are required for its full SUMOylation capacity. Finally, our functional analysis using reporter gene assays showed that SUMOylation may modulate transcriptional activity of FOXP2 in regulating downstream target genes (DISC1, SRPX2, and MiR200c). Altogether, we provide the first evidence that FOXP2 is a substrate for SUMOylation and SUMOylation of FOXP2 plays a functional role in regulating its transcriptional activity.

Indexed as

SumoylationAmino Acid SequenceAmino Acid SubstitutionConsensus SequenceForkhead Transcription FactorsHEK293 CellsHumansMCF-7 CellsMolecular Sequence DataPoint MutationProtein StabilitySUMO-1 ProteinTranscriptional ActivationForkhead Transcription FactorsFOXP2 protein, humanSUMO-1 ProteinFOXP2SUMOylationTRANSCRIPTIONAL ACTIVITY

Identifiers

PMID26212494
PMCPMC5696654
OpenAlexW1932307083

What OpenQuestion holds

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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.