Evidence map›Paper›PMID 16055503›Full record

ArticleMolecular biology of the cell2005

Phosphoproteome profiling of transforming growth factor (TGF)-beta signaling: abrogation of TGFbeta1-dependent phosphorylation of transcription factor-II-I (TFII-I) enhances cooperation of TFII-I and Smad3 in transcription.

Taras Stasyk, Anna Dubrovska, Marta Lomnytska, Ihor Yakymovych, Christer Wernstedt, Carl-Henrik Heldin, Ulf Hellman, Serhiy Souchelnytskyi

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. 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
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

17 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Hypoxia-activated Smad3-specific dephosphorylation by PP2A.The Journal of biological chemistry · 2010
    Article
  13. Understanding protein phosphorylation on a systems level.Briefings in functional genomics · 2010
    Review
  14. Article
  15. Article
  16. Article
  17. Identification of the TFII-I family target genes in the vertebrate genome.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
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

8 authors at 1 institution in 2 countries.

Taras StasykLudwig Institute for Cancer Research, Uppsala University, SE-751 24 Uppsala, Sweden.
Anna Dubrovska
Marta Lomnytska
Ihor Yakymovych
Christer Wernstedt
Carl-Henrik Heldin
Ulf Hellman
Serhiy Souchelnytskyi
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transforming growth factor-beta (TGFbeta) signaling involves activation of a number of signaling pathways, several of which are controlled by phosphorylation events. Here, we describe a phosphoproteome profiling of MCF-7 human breast epithelial cells treated with TGFbeta1. We identified 32 proteins that change their phosphorylation upon treatment with TGFbeta1; 26 of these proteins are novel targets of TGFbeta1. We show that Smad2 and Smad3 have different effects on the dynamics of TGFbeta1-induced protein phosphorylation. The identified proteins belong to nine functional groups, e.g., proteins regulating RNA processing, cytoskeletal rearrangements, and proteasomal degradation. To evaluate the proteomics findings, we explored the functional importance of TGFbeta1-dependent phosphorylation of one of the targets, i.e., transcription factor-II-I (TFII-I). We confirmed that TGFbeta1 stimulated TFII-I phosphorylation at serine residues 371 and 743. Abrogation of the phosphorylation by replacement of Ser371 and Ser743 with alanine residues resulted in enhanced complex formation between TFII-I and Smad3, and enhanced cooperation between TFII-I and Smad3 in transcriptional regulation, as evaluated by a microarray-based measurement of expression of endogenous cyclin D2, cyclin D3, and E2F2 genes, and by a luciferase reporter assay. Thus, TGFbeta1-dependent phosphorylation of TFII-I may modulate TGFbeta signaling at the transcriptional level.

Indexed as

Amino Acid SubstitutionCell Line, TumorCyclin D2Cyclin D3CyclinsE2F2 Transcription FactorHumansPhosphorylationProtein BindingProteomeSignal TransductionSmad2 ProteinSmad3 ProteinTranscription Factors, TFIITranscription, GeneticTransforming Growth Factor betaCCND2 protein, humanCCND3 protein, humanCyclin D2Cyclin D3CyclinsE2F2 protein, humanE2F2 Transcription FactorGTF2I protein, humanProteomeSmad2 ProteinSMAD2 protein, humanSmad3 ProteinSMAD3 protein, humanTGFB1 protein, humanTranscription Factors, TFIITransforming Growth Factor betaTransforming Growth Factor beta1

Identifiers

PMID16055503
PMCPMC1237082
OpenAlexW2133309812

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.