Evidence map›Paper›PMID 16478538›Full record

ArticleBMC biochemistry2006

Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its transcriptional activity.

Jungseog Kang, Christian B Gocke, Hongtao Yu

Open access · hybridAbstract readComparative Study
In one paragraph

Article in BMC biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  6. The role of SUMOylation during development.Biochemical Society transactions · 2020
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  14. Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016
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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 2 institutions in 1 country.

Jungseog KangDepartment of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, TX 75390-9041, USA. jungseog.kang@utsouthwestern.edu
Christian B Gocke
Hongtao Yu
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · US

Funding

Regulation of the Anaphase-Promoting Complex by the Spindle CheckpointR01GM061542 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI YU, HONGTAO · 2001 to 2010
$2.6M
NIGMS NIH HHS GM61542NIGMS NIH HHS R01 GM061542
6 · The paper itself

Abstract

backgroundSumoylation has emerged as an important posttranslational regulatory mechanism for transcription factors and cofactors. Sumoylation of many transcription factors represses their transcriptional activities. The myocyte enhancer factor 2 (MEF2) family of transcription factors plays an important role in regulating gene expression during myogenesis and has been recently shown to be sumoylated.

resultsConsistent with earlier reports, we show that sumoylation of MEF2C at K391 inhibits its transcriptional activity. Sumoylation of MEF2C does not block its DNA-binding activity. A small C-terminal fragment of MEF2C containing K391, referred to as delta-N2-MEF2C, is efficiently sumoylated and, when targeted to DNA, represses transcription at neighbouring promoters. Because delta-N2-MEF2C lacks the binding site for class II histone deacetylases (HDACs), this result suggests that sumoylation of MEF2C may help to recruit transcriptional repressors other than these HDACs. Intriguingly, we show that phosphorylation of S396 in MEF2C, a residue in close proximity to the major sumoylation site (K391) and known to be phosphorylated in vivo, enhances sumoylation of delta- N2-MEF2C in vitro. The S396A mutation reduces sumoylation of MEF2C in vivo and enhances the transcription activity of MEF2C in reporter assays.

conclusionWe propose that phosphorylation of MEF2C at S396 facilitates its sumoylation at K391, which in turn recruits yet unidentified co-repressors to inhibit transcription. Our studies further suggest that sumoylation motifs containing a phosphorylated serine or an acidic residue at the +5 position might be more efficiently sumoylated.

Indexed as

Protein Processing, Post-TranslationalTranscription, GeneticAmino Acid SequenceAmino Acid SubstitutionConsensus SequenceDesminHistone DeacetylasesHumansMADS Domain ProteinsMEF2 Transcription FactorsMolecular Sequence DataMyogenic Regulatory FactorsPhosphorylationPhosphoserinePromoter Regions, GeneticProtein BindingDesminHistone DeacetylasesMADS Domain ProteinsMEF2C protein, humanMEF2 Transcription FactorsMyogenic Regulatory FactorsPhosphoserineRecombinant Fusion ProteinsRepressor ProteinsSUMO-1 Protein

Identifiers

PMID16478538
PMCPMC1386686
OpenAlexW1844724534

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.