Evidence map›Paper›PMID 14597665›Full record

ArticleGenes & development2003

Smoothened transduces Hedgehog signal by physically interacting with Costal2/Fused complex through its C-terminal tail.

Jianhang Jia, Chao Tong, Jin Jiang

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
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

72 citing papers in PubMed, 171 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Hedgehog signaling mechanism and role in cancer.Seminars in cancer biology · 2022
    Review
  12. Review
  13. Cell-Based Assays for Smoothened Ubiquitination and Sumoylation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Gli Phosphorylation Code in Hedgehog Signal Transduction.Frontiers in cell and developmental biology · 2022
    Review
  15. Review
  16. Article
  17. Article
  18. Proteostasis in the Hedgehog signaling pathway.Seminars in cell & developmental biology · 2019
    Review
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Jianhang JiaCenter for Developmental Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9133, USA. jin.jiang@utsouthwestern.edu
Chao Tong
Jin Jiang
The University of Texas Southwestern Medical Center · USDevelopmental Studies Center · US

Funding

REGULATION OF HEDGEHOG SIGNALING IN DROSOPHILAR01GM061269 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, JIN · 2000 to 2016
$4.2M
Regulation of Hh/Ci signaling by Cos2 and its partnersR01GM067045 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, JIN · 2003 to 2015
$4.0M
NIGMS NIH HHS R01 GM061269NIGMS NIH HHS R01 GM067045
6 · The paper itself

Abstract

The Hedgehog (Hh) family of secreted proteins controls many aspects of growth and patterning in animal development. The seven-transmembrane protein Smoothened (Smo) transduces the Hh signal in both vertebrates and invertebrates; however, the mechanism of its action remains unknown. We found that Smo lacking its C-terminal tail (C-tail) is inactive, whereas membrane-tethered Smo C-tail has constitutive albeit low levels of Hh signaling activity. Smo physically interacts with Costal2 (Cos2) and Fused (Fu) through its C-tail. Deletion of the Cos2/Fu-binding domain from Smo abolishes its signaling activity. Moreover, overexpressing Cos2 mutants that fail to bind Fu and Ci but retain Smo-binding activity blocks Hh signaling. Taken together, our results suggest that Smo transduces the Hh signal by physically interacting with the Cos2/Fu protein complex.

Indexed as

AnimalsDrosophilaDrosophila ProteinsHedgehog ProteinsKinesinsMutationProtein Serine-Threonine KinasesReceptors, G-Protein-CoupledSequence DeletionSignal TransductionSmoothened Receptorcos protein, DrosophilaDrosophila Proteinsfu protein, DrosophilaHedgehog Proteinshh protein, DrosophilaKinesinsProtein Serine-Threonine KinasesReceptors, G-Protein-CoupledSmoothened Receptorsmo protein, Drosophila

Identifiers

PMID14597665
PMCPMC280620
OpenAlexW2085938413

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.