Evidence map›Paper›PMID 32152405›Full record

ArticleOncogene2020

The non-receptor tyrosine phosphatase type 14 blocks caveolin-1-enhanced cancer cell metastasis.

Natalia I Díaz-Valdivia, Jorge Díaz, Pamela Contreras, América Campos, Victoria Rojas-Celis, Renato A Burgos-Ravanal, Lorena Lobos-González, Vicente A Torres, Viviana I Perez, Balz Frei and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Oncogene, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
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  10. RETRACTED: The p53-Driven Anticancer Effect ofLife (Basel, Switzerland) · 2022
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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

12 authors at 4 institutions in 2 countries.

Natalia I Díaz-ValdiviaCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Jorge DíazCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Pamela ContrerasCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
América CamposCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Victoria Rojas-CelisCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Renato A Burgos-RavanalCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Lorena Lobos-GonzálezCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile.
Vicente A TorresInstitute for Research in Dental Science, Faculty of Dentistry, Universidad de Chile, Santiago, Chile.ORCID http://orcid.org/0000-0002-5973-7248
Viviana I PerezDepartment of Biochemistry and Biophysics, Linus Pauling Institute, Oregon State University, Corvallis, OR, USA.
Balz FreiDepartment of Biochemistry and Biophysics, Linus Pauling Institute, Oregon State University, Corvallis, OR, USA.
Lisette LeytonCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile. lleyton@med.uchile.cl.
Andrew F G QuestCellular Communication Laboratory, Center for studies on Exercise, Metabolism and Cancer (CEMC), Advanced Center for Chronic Diseases (ACCDiS), Faculty of Medicine, Universidad de Chile, Santiago, Chile. aquest@med.uchile.cl.
Advanced Center for Chronic Diseases · CLFundación Ciencia and Vida · CLOregon State University · USUniversity of Chile · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caveolin-1 (CAV1) enhanced migration, invasion, and metastasis of cancer cells is inhibited by co-expression of the glycoprotein E-cadherin. Although the two proteins form a multiprotein complex that includes β-catenin, it remained unclear how this would contribute to blocking the metastasis promoting function of CAV1. Here, we characterized by mass spectrometry the protein composition of CAV1 immunoprecipitates from B16F10 murine melanoma cells expressing or not E-cadherin. The novel protein tyrosine phosphatase PTPN14 was identified by mass spectrometry analysis exclusively in co-immunoprecipitates of CAV1 with E-cadherin. Interestingly, PTPN14 is implicated in controlling metastasis, but only few known PTPN14 substrates exist. We corroborated by western blotting experiments that PTPN14 and CAV1 co-inmunoprecipitated in the presence of E-cadherin in B16F10 melanoma and other cancer cells. Moreover, the CAV1(Y14F) mutant protein was shown to co-immunoprecipitate with PTPN14 even in the absence of E-cadherin, and overexpression of PTPN14 reduced CAV1 phosphorylation on tyrosine-14, as well as suppressed CAV1-enhanced cell migration, invasion and Rac-1 activation in B16F10, metastatic colon [HT29(US)] and breast cancer (MDA-MB-231) cell lines. Finally, PTPN14 overexpression in B16F10 cells reduced the ability of CAV1 to induce metastasis in vivo. In summary, we identify here CAV1 as a novel substrate for PTPN14 and show that overexpression of this phosphatase suffices to reduce CAV1-induced metastasis.

Indexed as

Animalsbeta CateninCadherinsCaveolin 1Cell Line, TumorCell MovementCell ProliferationFemaleGene Expression Regulation, NeoplasticHumansMelanoma, ExperimentalMiceNeoplasm InvasivenessNeoplasm MetastasisPhosphorylationProtein Tyrosine Phosphatases, Non-Receptorbeta CateninCadherinsCav1 protein, mouseCaveolin 1CTNNB1 protein, mouseProtein Tyrosine Phosphatases, Non-ReceptorPTPN14 protein, mouse

Identifiers

PMID32152405
PMCPMC7190567
OpenAlexW3009750257

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.