Evidence map›Paper›PMID 14614827›Full record

ArticleCurrent biology : CB2003

Identification of a functional interaction between the transmembrane protein Smoothened and the kinesin-related protein Costal2.

Stacey K Ogden, Manuel Ascano, Melanie A Stegman, Liza M Suber, Joan E Hooper, David J Robbins

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Current biology : CB, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Hedgehog signaling mechanism and role in cancer.Seminars in cancer biology · 2022
    Review
  7. Proteostasis in the Hedgehog signaling pathway.Seminars in cell & developmental biology · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
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  13. G-protein-coupled receptors, Hedgehog signaling and primary cilia.Seminars in cell & developmental biology · 2014
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
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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 1 country.

Stacey K OgdenDepartment of Pharmacology and Toxicology, Dartmouth Medical School, 7650 Remsen Hall, Hanover, NH 03755, USA.
Manuel Ascano
Melanie A Stegman
Liza M Suber
Joan E Hooper
David J Robbins
Dartmouth College · USUniversity of Cincinnati · USUniversity of Colorado Hospital · US

Funding

ENVIRONMETAL CARCINOGENESIS AND MUTAGENESIST32ES007250 · NIEHS · UNIVERSITY OF CINCINNATI · PI MILLER, WILLIAM E · 1988 to 2024
$11.9M
RECONSTITUTION OF HEDGEHOG SIGNALING COMPLEXR01CA082628 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI ROBBINS, DAVID J · 1999 to 2014
$4.1M
NCI NIH HHS CA 82628NCI NIH HHS R01 CA082628NIEHS NIH HHS 5T32 ES 07250NIEHS NIH HHS T32 ES007250NIGMS NIH HHS GM 4539
6 · The paper itself

Abstract

The hedgehog (Hh) family of morphogens plays important instructional roles in the development of numerous metazoan structures. Consistent with the role Hh homologs play in cell fate determination, aberrant Hh signaling results in numerous human pathologies. Hh signal transduction is initiated when Hh binds to its receptor Patched (Ptc), activating the transmembrane protein Smoothened (Smo). Smo transmits its activation signal to a microtubule-associated Hedgehog signaling complex (HSC). At a minimum, the HSC consists of the Kinesin-related protein Costal2 (Cos2), the protein kinase Fused (Fu), and the transcription factor Cubitus interruptus (Ci). In response to HSC activation, the ratio between repressor and activator forms of Ci is altered, determining the expression levels of various Hh target genes. The steps between Smo activation and signaling to the HSC have not been described. Here, we describe a functional interaction between Smo and Cos2, which is necessary for Hh signaling. We propose that this interaction is direct and allows for activation of Ci in response to Hh. This work fills in the last major gap in our understanding of the Hh signal transduction pathway by suggesting that no intermediate signal is required to connect Smo to the HSC.

Indexed as

Drosophila ProteinsSignal TransductionAnimalsAnimals, Genetically ModifiedBlotting, WesternDrosophilaKinesinsMicroscopy, FluorescencePrecipitin TestsReceptors, G-Protein-CoupledSmoothened ReceptorTwo-Hybrid System Techniquescos protein, DrosophilaDrosophila ProteinsKinesinsReceptors, G-Protein-CoupledSmoothened Receptorsmo protein, Drosophila

Identifiers

PMID14614827
PMCPMC3711143
OpenAlexW2029500889

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.