Evidence map›Paper›PMID 36672319›Full record

ArticleCancers2023

Partial Truncation of the C-Terminal Domain of PTCH1 in Cancer Enhances Autophagy and Metabolic Adaptability.

Begoña Caballero-Ruiz, Danai S Gkotsi, Hattie Ollerton, Cintli C Morales-Alcala, Rosa Bordone, Georgia M L Jenkins, Laura Di Magno, Gianluca Canettieri, Natalia A Riobo-Del Galdo

Open access · goldAbstract read
In one paragraph

Article in Cancers, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. 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

9 authors at 3 institutions in 2 countries.

Begoña Caballero-RuizDepartment of Molecular Medicine, Sapienza University of Rome, 00161 Rome, Italy.ORCID 0000-0001-5278-5573
Danai S GkotsiSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS29JT, UK.
Hattie OllertonSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS29JT, UK.
Cintli C Morales-AlcalaLeeds Institute for Medical Research, School of Medicine, University of Leeds, Leeds LS29JT, UK.
Rosa BordoneDepartment of Molecular Medicine, Sapienza University of Rome, 00161 Rome, Italy.
Georgia M L JenkinsSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS29JT, UK.
Laura Di MagnoDepartment of Molecular Medicine, Sapienza University of Rome, 00161 Rome, Italy.ORCID 0000-0001-9446-8752
Gianluca CanettieriDepartment of Molecular Medicine, Sapienza University of Rome, 00161 Rome, Italy.ORCID 0000-0001-6694-2613
Natalia A Riobo-Del GaldoSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS29JT, UK.ORCID 0000-0002-8942-7873
University of Leeds · GBSapienza University of Rome · ITIstituto Pasteur · IT

Funding

Biotechnology and Biological Sciences Research Council BB/S01716X/1Dipartimenti di Eccellenza L. 232/2016Fondazione Umberto Veronesi fellowship to L.D.MIstituto Pasteur Fondazione Cenci BolognettiItalian Association for Cancer Research IG25833Sapienza University of Rome RG12117A61923A6F
6 · The paper itself

Abstract

The Hedgehog receptor, Patched1 (PTCH1), is a well-known tumour suppressor. While the tumour suppressor's activity is mostly ascribed to its function as a repressor of the canonical Smoothened/Gli pathway, its C-terminal domain (CTD) was reported to have additional non-canonical functions. One of them is the reduction of autophagic flux through direct interaction with the Unc-51, like the autophagy activating kinase (ULK) complex subunit autophagy-related protein-101 (ATG101). With the aim of investigating whether this function of PTCH1 is important in cancer cell fitness, we first identified frameshift mutations in the CTD of PTCH1 in cancer databases. We demonstrated that those mutations disrupt PTCH1 interaction with ATG101 and increase autophagic flux. Using deletion mutants of the PTCH1 CTD in co-immunoprecipitation studies, we established that the 1309-1447 region is necessary and sufficient for interaction with ATG101. We next showed that the three most common PTCH1 CTD mutations in endometrial, stomach and colon adenocarcinomas that cause frameshifts at S1203, R1308 and Y1316 lack the ability to interact with ATG101 and limit autophagic flux, determined by bafilomycin A1-sensitive accumulation of the autophagy markers LC3BII and p62. We next engineered PTCH1 indel mutations at S1223 by CRISPR/Cas9 in SW620 colon cancer cells. Comparison of two independent clones harbouring PTCH1 S1223fs mutations to their isogenic parental cell lines expressing wild-type PTCH1 showed a significant increase in basal and rapamycin-stimulated autophagic flux, as predicted by loss of ATG101 interaction. Furthermore, the PTCH1 CTD mutant cells displayed increased proliferation in the presence of rapamycin and reduced sensitivity to glycolysis inhibitors. Our findings suggest that loss of the PTCH1-ATG101 interaction by mutations in the CTD of PTCH1 in cancer might confer a selective advantage by stimulating autophagy and facilitating adaptation to nutrient deprivation conditions.

Indexed as

ATG101autophagycancerglycolysisHedgehogPTCH1

Identifiers

PMID36672319
PMCPMC9856372
OpenAlexW4313646951

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.