Evidence map›Paper›PMID 21990430›Full record

ArticleScience signaling2011

Phosphorylation of Mad controls competition between wingless and BMP signaling.

Edward Eivers, Hadrien Demagny, Renee H Choi, Edward M De Robertis

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. TGF-β Family Signaling inCold Spring Harbor perspectives in biology · 2017
    Review
  7. Signaling Cross Talk between TGF-β/Smad and Other Signaling Pathways.Cold Spring Harbor perspectives in biology · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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  14. Article
  15. Review
  16. Article
  17. Article
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  20. 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

4 authors at 2 institutions in 1 country.

Edward EiversHoward Hughes Medical Institute and Department of Biological Chemistry, University of California, Los Angeles, CA 90095-1662, USA.
Hadrien Demagny
Renee H Choi
Edward M De Robertis
Howard Hughes Medical Institute · USUniversity of California, Los Angeles · US

Funding

HOMEOBOX GENES AND THEIR TARGETS IN XENOPUS DEVELOPMENTR37HD021502 · NICHD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DE ROBERTIS, EDWARD M · 1997 to 2006
$2.2M
HOMEOBOXES IN XENOPUS DEVELOPMENTR01HD021502 · NICHD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DE ROBERTIS, EDWARD M · 1986 to 2011
$1.6M
Howard Hughes Medical InstituteNICHD NIH HHS HD21502-25NICHD NIH HHS R01 HD021502NICHD NIH HHS R37 HD021502
6 · The paper itself

Abstract

Bone morphogenetic proteins (BMPs) and Wnts are growth factors that provide essential patterning signals for cell proliferation and differentiation. Here, we describe a molecular mechanism by which the phosphorylation state of the Drosophila transcription factor Mad determines its ability to transduce either BMP or Wingless (Wg) signals. Previously, Mad was thought to function in gene transcription only when phosphorylated by BMP receptors. We found that the unphosphorylated form of Mad was required for canonical Wg signaling by interacting with the Pangolin-Armadillo transcriptional complex. Phosphorylation of the carboxyl terminus of Mad by BMP receptor directed Mad toward BMP signaling, thereby preventing Mad from functioning in the Wg pathway. The results show that Mad has distinct signal transduction roles in the BMP and Wnt pathways depending on its phosphorylation state.

Indexed as

Models, BiologicalAnimalsBone Morphogenetic ProteinsCell LineCloning, MolecularDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsGene SilencingGlycogen Synthase Kinase 3HumansImmunoprecipitationLarvaPhosphorylationPolyubiquitinRepressor ProteinsBone Morphogenetic ProteinsDNA-Binding ProteinsDrosophila ProteinsGlycogen Synthase Kinase 3MAD protein, Drosophilapan protein, DrosophilaPolyubiquitinRepressor ProteinsSgg protein, DrosophilaTranscription Factorswg protein, DrosophilaWnt1 Protein

Identifiers

PMID21990430
PMCPMC3215398
OpenAlexW2110658264

What OpenQuestion holds

Textmetadata
LicenceTDM
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.