Evidence map›Paper›PMID 12221285›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes.

Marco Gallio, Gwen Sturgill, Philip Rather, Per Kylsten

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 113 citations in OpenAlex.

  1. Microorganisms · 2022
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structure and mechanism of rhomboid protease.The Journal of biological chemistry · 2013
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The PARL family of mitochondrial rhomboid proteases.Seminars in cell & developmental biology · 2010
    Review
  16. Review
  17. Review
  18. Review
  19. Structure and mechanism of intramembrane protease.Seminars in cell & developmental biology · 2009
    Review
  20. Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated transactivation of EGFR growth signals in head and neck squamous cancer cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    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

4 authors at 3 institutions in 2 countries.

Marco GallioDepartment of Medical Nutrition, Karolinska Institute, Huddinge, Sweden. marco.gallio@sh.se
Gwen Sturgill
Philip Rather
Per Kylsten
Case Western Reserve University · USKarolinska Institutet · SESödertörn University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epidermal growth factor receptor (EGFr) is a key mediator of cell communication during animal development and homeostasis. In Drosophila, the signaling event is commonly regulated by the polytopic membrane protein Rhomboid (RHO), which mediates the proteolytic activation of EGFr ligands, allowing the secretion of the active signal. Until very recently, the biochemical function of RHO had remained elusive. It is now believed that Drosophila RHO is the founder member of a previously undescribed family of serine proteases, and that it could be directly responsible for the unusual, intramembranous cleavage of EGFr ligands. Here we show that the function of RHO is conserved in Gram-negative bacteria. AarA, a Providencia stuartii RHO-related protein, is active in Drosophila on the fly EGFr ligands. Vice versa, Drosophila RHO-1 can effectively rescue the bacterium's ability to produce or release the signal that activates density-dependent gene regulation (or quorum sensing). This study provides the first evidence that prokaryotic and eukaryotic RHOs could have a conserved role in cell communication and that their biochemical properties could be more similar than previously anticipated.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsConserved SequenceDrosophila melanogasterDrosophila ProteinsErbB ReceptorsEvolution, MolecularHumansLigandsMembrane ProteinsModels, BiologicalMolecular Sequence DataPhylogenyProvidenciaRepressor ProteinsaarA protein, Providencia stuartiiBacterial ProteinsDrosophila ProteinsErbB ReceptorsLigandsMembrane ProteinsRepressor ProteinsRho protein, DrosophilaSerine EndopeptidasesStet protein, Drosophila

Identifiers

PMID12221285
PMCPMC129423
OpenAlexW2136394802

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.