Evidence map›Paper›PMID 24608521›Full record

ArticlePloS one2014

Attenuation of hedgehog acyltransferase-catalyzed sonic Hedgehog palmitoylation causes reduced signaling, proliferation and invasiveness of human carcinoma cells.

Antonios D Konitsiotis, Shu-Chun Chang, Biljana Jovanović, Paulina Ciepla, Naoko Masumoto, Christopher P Palmer, Edward W Tate, John R Couchman, Anthony I Magee

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

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  19. Chemical reporters for exploring protein acylation.Biochemical Society transactions · 2015
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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

9 authors at 3 institutions in 2 countries.

Antonios D KonitsiotisMolecular Medicine Section, National Heart & Lung Institute, Imperial College London, London, United Kingdom.
Shu-Chun ChangMolecular Medicine Section, National Heart & Lung Institute, Imperial College London, London, United Kingdom.
Biljana JovanovićMolecular Medicine Section, National Heart & Lung Institute, Imperial College London, London, United Kingdom.
Paulina CieplaDepartment of Chemistry, Imperial College London, London, United Kingdom; Institute of Chemical Biology, Imperial College London, London, United Kingdom.
Naoko MasumotoDepartment of Chemistry, Imperial College London, London, United Kingdom; Institute of Chemical Biology, Imperial College London, London, United Kingdom.
Christopher P PalmerInstitute for Health Research and Policy, London Metropolitan University, London, United Kingdom.
Edward W TateDepartment of Chemistry, Imperial College London, London, United Kingdom; Institute of Chemical Biology, Imperial College London, London, United Kingdom.
John R CouchmanDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.
Anthony I MageeMolecular Medicine Section, National Heart & Lung Institute, Imperial College London, London, United Kingdom; Institute of Chemical Biology, Imperial College London, London, United Kingdom.
Imperial College London · GBLondon Metropolitan University · GBUniversity of Copenhagen · DK

Funding

Biotechnology and Biological Sciences Research Council BB/D02014X/1Cancer Research UK 16402Medical Research Council G0700771
6 · The paper itself

Abstract

Overexpression of Hedgehog family proteins contributes to the aetiology of many cancers. To be highly active, Hedgehog proteins must be palmitoylated at their N-terminus by the MBOAT family multispanning membrane enzyme Hedgehog acyltransferase (Hhat). In a pancreatic ductal adenocarcinoma (PDAC) cell line PANC-1 and transfected HEK293a cells Hhat localized to the endoplasmic reticulum. siRNA knockdown showed that Hhat is required for Sonic hedgehog (Shh) palmitoylation, for its assembly into high molecular weight extracellular complexes and for functional activity. Hhat knockdown inhibited Hh autocrine and juxtacrine signaling, and inhibited PDAC cell growth and invasiveness in vitro. In addition, Hhat knockdown in a HEK293a cell line constitutively expressing Shh and A549 human non-small cell lung cancer cells inhibited their ability to signal in a juxtacrine/paracrine fashion to the reporter cell lines C3H10T1/2 and Shh-Light2. Our data identify Hhat as a key player in Hh-dependent signaling and tumour cell transformed behaviour.

Indexed as

AcyltransferasesCarcinoma, Pancreatic DuctalCell Line, TumorCell ProliferationHedgehog ProteinsHumansLipoylationSignal TransductionAcyltransferasesHedgehog ProteinsHHAT protein, human

Identifiers

PMID24608521
PMCPMC3946499
OpenAlexW2070149860

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.