Evidence map›Paper›PMID 23637228›Full record

ArticleThe Journal of biological chemistry2013

Sumoylation of the basic helix-loop-helix transcription factor sharp-1 regulates recruitment of the histone methyltransferase G9a and function in myogenesis.

Yaju Wang, Shilpa Rani Shankar, Devaki Kher, Belinda Mei Tze Ling, Reshma Taneja

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Approach to Functions ofInternational journal of molecular sciences · 2023
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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

5 authors at 1 institution in 1 country.

Yaju WangDepartment of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, 117597, Singapore.
Shilpa Rani Shankar
Devaki Kher
Belinda Mei Tze Ling
Reshma Taneja
National University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sumoylation is an important post-translational modification that alters the activity of many transcription factors. However, the mechanisms that link sumoylation to alterations in chromatin structure, which culminate in tissue specific gene expression, are not fully understood. In this study, we demonstrate that SUMO modification of the transcription factor Sharp-1 is required for its full transcriptional repression activity and function as an inhibitor of skeletal muscle differentiation. Sharp-1 is modified by sumoylation at two conserved lysine residues 240 and 255. Mutation of these SUMO acceptor sites in Sharp-1 does not impact its subcellular localization but attenuates its ability to act as a transcriptional repressor and inhibit myogenic differentiation. Consistently, co-expression of the SUMO protease SENP1 with wild type Sharp-1 abrogates Sharp-1-dependent inhibition of myogenesis. Interestingly, sumoylation acts as a signal for recruitment of the co-repressor G9a. Thus, enrichment of G9a, and histone H3 lysine 9 dimethylation (H3K9me2), a signature of G9a activity, is dramatically reduced at muscle promoters in cells expressing sumoylation-defective Sharp-1. Our findings demonstrate how sumoylation of Sharp-1 exerts an impact on chromatin structure and transcriptional repression of muscle gene expression through recruitment of G9a.

Indexed as

Cell DifferentiationSumoylationAmino Acid SequenceAnimalsBasic Helix-Loop-Helix ProteinsBinding SitesCell LineChlorocebus aethiopsConserved SequenceCOS CellsCysteine EndopeptidasesEndopeptidasesHEK293 CellsHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansBasic Helix-Loop-Helix ProteinsBHLHE41 protein, humanCysteine EndopeptidasesEHMT2 protein, humanEndopeptidasesHistocompatibility AntigensHistone-Lysine N-MethyltransferaseMyoD1 myogenic differentiation proteinMyoD ProteinSENP1 protein, humanChromatin ModificationDifferentiationEpigeneticsHelix-Loop-Helix Transcription FactorsHistone MethylationMyogenesisSkeletal MuscleSumoylationTranscription Factors

Identifiers

PMID23637228
PMCPMC3682566
OpenAlexW2083348570

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.