Evidence map›Paper›PMID 19491097›Full record

ArticleThe Journal of biological chemistry2009

GCN5-mediated transcriptional control of the metabolic coactivator PGC-1beta through lysine acetylation.

Timothy J Kelly, Carles Lerin, Wilhelm Haas, Steven P Gygi, Pere Puigserver

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

78 citing papers in PubMed, 129 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Review
  6. Molecular mechanisms of mitochondrial quality control.Translational neurodegeneration · 2025
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Contributions of transcriptional noise to leukaemia evolution: KAT2A as a case-study.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. PGC-1Frontiers in cell and developmental biology · 2022
    Review
  19. Review
  20. Article

18 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Timothy J KellyFrom the Department of Cancer Biology, Dana-Farber Cancer Institute, Harvad Medical School, Boston, Massachusetts 02115, USA.
Carles Lerin
Wilhelm Haas
Steven P Gygi
Pere Puigserver
Harvard University · USDana-Farber Cancer Institute · USJohns Hopkins University · US

Funding

Control of Nutrient Homeostasis through PGC-1alpha and SIRT1R01DK069966 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI PUIGSERVER, PERE · 2005 to 2014
$4.2M
NIDDK NIH HHS R01 DK069966
6 · The paper itself

Abstract

Changes in expression levels of genes encoding for proteins that control metabolic pathways are essential to maintain nutrient and energy homeostasis in individual cells as well as in organisms. An important regulated step in this process is accomplished through covalent chemical modifications of proteins that form complexes with the chromatin of gene promoters. The peroxisome proliferators gamma co-activator 1 (PGC-1) family of transcriptional co-activators comprises important components of a number of these complexes and participates in a large array of glucose and lipid metabolic adaptations. Here, we show that PGC-1beta is acetylated on at least 10 lysine residues distributed along the length of the protein by the acetyl transferase general control of amino-acid synthesis (GCN5) and that this acetylation reaction is reversed by the deacetylase sirtuin 1 (SIRT1). GCN5 strongly interacts with PGC-1beta and represses its transcriptional activity associated with transcription factors such as ERRalpha, NRF-1, and HNF4alpha, however acetylation and transcriptional repression do not occur when a catalytically inactive GCN5 is co-expressed. Transcriptional repression coincides with PGC-1beta redistribution to nuclear foci where it co-localizes with GCN5. Furthermore, knockdown of GCN5 ablates PGC-1beta acetylation and increases transcriptional activity. In primary skeletal muscle cells, PGC-1beta induction of endogenous target genes, including MCAD and GLUT4, is largely repressed by GCN5. Functionally, this translates to a blunted response to PGC-1beta-induced insulin-mediated glucose transport. These results suggest that PGC-1beta acetylation by GCN5 might be an important step in the control of glucose and lipid pathways and its dysregulation could contribute to metabolic diseases.

Indexed as

Transcriptional ActivationAcetylationAcetyltransferasesAmino Acid SequenceBiological TransportCarrier ProteinsCell NucleusCells, CulturedGene Expression RegulationGlucoseHistone AcetyltransferasesHumansInsulinKidneyLysineMolecular Sequence DataAcetyltransferasesCarrier ProteinsGlucoseHistone AcetyltransferasesInsulinKAT2A protein, humanLysinep300-CBP-Associated FactorPPARGC1B protein, humanRNA-Binding Proteins

Identifiers

PMID19491097
PMCPMC2740420
OpenAlexW2034175329

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.