Evidence map›Paper›PMID 25404345›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation.

Jose C Paz, Sangho Park, Naomi Phillips, Shigenobu Matsumura, Wen-Wei Tsai, Lawryn Kasper, Paul K Brindle, Guangtao Zhang, Ming-Ming Zhou, Peter E Wright and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Multi-faceted regulation of CREB family transcription factors.Frontiers in molecular neuroscience · 2024
    Review
  6. Article
  7. Article
  8. CREB1ACS omega · 2021
    Article
  9. What turns CREB on? And off? And why does it matter?Cellular and molecular life sciences : CMLS · 2020
    Review
  10. Review
  11. Article
  12. Procyanidins and Alzheimer's Disease.Molecular neurobiology · 2019
    Review
  13. Functions and mechanisms of non-histone protein acetylation.Nature reviews. Molecular cell biology · 2019
    Review
  14. Review
  15. Adipose tissue NADBioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  16. Article
  17. 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

11 authors at 4 institutions in 1 country.

Jose C PazPeptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, CA 92037;
Sangho ParkDepartment of Integrative Structural and Computational Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037;
Naomi PhillipsPeptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, CA 92037;
Shigenobu MatsumuraPeptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, CA 92037;
Wen-Wei TsaiPeptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, CA 92037;
Lawryn KasperDepartment of Biochemistry, St. Jude Children's Research Hospital, Memphis, TN 38105; and.
Paul K BrindleDepartment of Biochemistry, St. Jude Children's Research Hospital, Memphis, TN 38105; and.
Guangtao ZhangDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
Ming-Ming ZhouDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
Peter E WrightDepartment of Integrative Structural and Computational Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037;
Marc MontminyPeptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, CA 92037; montminy@salk.edu.
Salk Institute for Biological Studies · USIcahn School of Medicine at Mount Sinai · USScripps Research Institute · USSt. Jude Children's Research Hospital · US

Funding

Regulation of Hepatic Gluconeogenesis by the CREB:TORC2 PathwayR37DK083834 · NIDDK · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI MONTMINY, MARC R · 2010 to 2018
$6.4M
Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
Role of the TORC/CRTC Family of Coactivators in Energy BalanceR01DK049777 · NIDDK · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI MONTMINY, MARC R · 1995 to 2014
$5.6M
Regulation of Hepatic Gluconeogenesis by the CREB:TORC2 PathwayR01DK083834 · NIDDK · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI MONTMINY, MARC R · 2009 to 2022
$3.7M
NCI NIH HHS R01 CA096865NCI NIH HHS R01-CA096865NIDDK NIH HHS R01 DK049777NIDDK NIH HHS R01-DK049777NIDDK NIH HHS R01 DK083834NIDDK NIH HHS R01-DK083834NIDDK NIH HHS R37 DK083834
6 · The paper itself

Abstract

In the fasted state, increases in catecholamine signaling promote adipocyte function via the protein kinase A-mediated phosphorylation of cyclic AMP response element binding protein (CREB). CREB activity is further up-regulated in obesity, despite reductions in catecholamine signaling, where it contributes to the development of insulin resistance. Here we show that obesity promotes the CREB binding protein (CBP)-mediated acetylation of CREB at Lys136 in adipose. Under lean conditions, CREB acetylation was low due to an association with the energy-sensing NAD(+)-dependent deacetylase SirT1; amounts of acetylated CREB were increased in obesity, when SirT1 undergoes proteolytic degradation. Whereas CREB phosphorylation stimulated an association with the KIX domain of CBP, Lys136 acetylation triggered an interaction with the CBP bromodomain (BRD) that augmented recruitment of this coactivator to the promoter. Indeed, coincident Ser133 phosphorylation and Lys136 acetylation of CREB stimulated the formation of a ternary complex with the KIX and BRD domains of CBP by NMR analysis. As disruption of the CREB:BRD complex with a CBP-specific BRD inhibitor blocked effects of CREB acetylation on target gene expression, our results demonstrate how changes in nutrient status modulate cellular gene expression in response to hormonal signals.

Indexed as

Signal Transduction3T3-L1 CellsAcetylationAdipocytesAnimalsCells, CulturedCREB-Binding ProteinCyclic AMP Response Element-Binding ProteinEmbryo, MammalianFibroblastsGene Expression ProfilingHEK293 CellsHumansImmunoblottingLysineMiceCREB-Binding ProteinCyclic AMP Response Element-Binding ProteinLysineSirt1 protein, mouseSirtuin 1acetylationCBPCREBphosphorylationSirT1

Identifiers

PMID25404345
PMCPMC4260582
OpenAlexW1989044720

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.