Evidence map›Paper›PMID 16615205›Full record

ArticleProceedings. Biological sciences2006

An unusual choanoflagellate protein released by Hedgehog autocatalytic processing.

Elizabeth A Snell, Nina M Brooke, William R Taylor, Didier Casane, Hervé Philippe, Peter W H Holland

Open access · greenAbstract read
In one paragraph

Article in Proceedings. Biological sciences, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Phylogenetic evidence for the modular evolution of metazoan signalling pathways.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Degenerate evolution of the hedgehog gene in a hemichordate lineage.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Hedgehog protein family.Genome biology · 2008
    Review
  18. The primary cilium at the crossroads of mammalian hedgehog signaling.Current topics in developmental biology · 2008
    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

6 authors at 3 institutions in 4 countries.

Elizabeth A SnellSchool of Animal and Microbial Sciences, The University of Reading, Whiteknights, Reading RG6 6AJ, UK.
Nina M Brooke
William R Taylor
Didier Casane
Hervé Philippe
Peter W H Holland
Centre National de la Recherche Scientifique · FRUniversity of Oxford · GBNorth Carolina Agricultural and Technical State University · US

Funding

Medical Research Council MC_U117581331
6 · The paper itself

Abstract

Hedgehog proteins are important cell-cell signalling proteins utilized during the development of multicellular animals. Members of the hedgehog gene family have not been detected outside the Metazoa, raising unanswered questions about their evolutionary origin. Here we report a highly unusual hedgehog-related gene from a choanoflagellate, a close unicellular relative of the animals. The deduced C-terminal domain, Hoglet-C, is homologous to the autocatalytic domain of Hedgehog proteins and is predicted to function in autocatalytic cleavage of the precursor peptide. In contrast, the N-terminal Hoglet-N peptide has no similarity to the signalling peptide of Hedgehog (Hh-N). Instead, Hoglet-N is deduced to be a secreted protein with an enormous threonine-rich domain of unprecedented size and purity (over 200 threonine residues) and two polysaccharide-binding domains. Structural modelling reveals that these domains have a novel combination of features found in cellulose-binding domains (CBD) of types IIa and IIb, and are expected to bind cellulose. We propose that the two CBD domains enable Hoglet-N to bind to plant matter, tethering an amorphous nucleophilic anchor, facilitating transient adhesion of the choanoflagellate cell. Since Hh-C and Hoglet-C are homologous, but Hh-N and Hoglet-N are not, we argue that metazoan hedgehog genes evolved by fusion of two distinct genes.

Indexed as

Amino Acid SequenceAnimalsBase SequenceDNA, ProtozoanEukaryotic CellsModels, MolecularMolecular Sequence DataPhylogenyProteinsRandom Amplified Polymorphic DNA TechniqueSequence AlignmentSequence Analysis, DNADNA, ProtozoanProteins

Identifiers

PMID16615205
PMCPMC1560198
OpenAlexW2113506067

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.