Evidence map›Paper›PMID 14645371›Full record

ArticleThe Journal of biological chemistry2004

The Kinesin-related protein Costal2 associates with membranes in a Hedgehog-sensitive, Smoothened-independent manner.

Melanie A Stegman, John A Goetz, Manuel Ascano, Stacey K Ogden, Kent E Nybakken, David J Robbins

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2004. 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
2.5field-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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
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  6. Unconventional functions of microtubule motors.Archives of biochemistry and biophysics · 2012
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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 4 institutions in 2 countries.

Melanie A StegmanDepartment of Pharmacology and Toxicology, Dartmouth Medical School, Hanover, New Hampshire 03755-3835, USA.
John A Goetz
Manuel Ascano
Stacey K Ogden
Kent E Nybakken
David J Robbins
Dartmouth College · USDartmouth Hospital · GBHoward Hughes Medical Institute · USUniversity of Cincinnati · 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 CA82628NCI NIH HHS R01 CA082628NIEHS NIH HHS 5-T32 ES07250NIEHS NIH HHS T32 ES007250
6 · The paper itself

Abstract

In Drosophila, Hedgehog (Hh) signal transduction has been shown to require a multiprotein complex (Hedgehog signaling complex (HSC)), which includes the Kinesin-related protein Costal2 (Cos2), the serine/threonine protein kinase Fused (Fu), and the transcription factor Cubitus interruptus (Ci). We present evidence that a biologically relevant fraction of the HSC is found in association with cellular membranes. We demonstrate that Cos2 is capable of tethering an exogenous protein to vesicular membranes and that Cos2 association with membranes is Hh-sensitive. In addition, we demonstrate that Cos2 associates with membranes in cells that lack the transmembrane protein Smoothened (Smo) through a domain of Cos2 distinct from its recently characterized Smo binding domain. We suggest that an Hh-regulated membrane binding activity of Cos2 is part of the mechanism by which Cos2 contributes to Hh signaling. We propose a model in which there are two distinct HSCs with discrete subcellular localizations and activities: one is endosome-associated and facilitates production of a repressor form of Ci (HSC-R), and one is Smo-associated and promotes Ci activation (HSC-A). In response to Hh and through interaction with Cos2, Smo mediates both inhibition of the endosome-associated HSC-R and activation of HSC-A at the plasma membrane.

Indexed as

AnimalsCell LineCell MembraneCentrifugation, Density GradientDNADNA-Binding ProteinsDose-Response Relationship, DrugDrosophilaDrosophila ProteinsElectrophoresis, Polyacrylamide GelEndosomesGenes, ReporterGreen Fluorescent ProteinsHedgehog ProteinsImmunoblottingKinesinsci protein, Drosophilacos protein, DrosophilaDNADNA-Binding ProteinsDrosophila Proteinsfu protein, DrosophilaGreen Fluorescent ProteinsHedgehog Proteinshh protein, DrosophilaKinesinsLuminescent ProteinsProtein Serine-Threonine KinasesReceptors, G-Protein-CoupledRNA, Double-StrandedSmoothened Receptorsmo protein, DrosophilaTranscription Factors

Identifiers

PMID14645371
PMCPMC3659396
OpenAlexW2020588466

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.