PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN

Cancer and Parkinson disease (PD) derive from distinct alterations in cellular processes, yet there are pathogenic mutations that are unequivocally linked to both diseases. Here we expand on our recent findings that loss of parkin RBR E3 ubiquitin protein ligase (PRKN, best known as PARK2)—which is...

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Autores principales: Gupta, Amit, Anjomani-Virmouni, Sara, Koundouros, Nikos, Poulogiannis, George
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Author's View
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706935/
https://www.ncbi.nlm.nih.gov/pubmed/29209642
http://dx.doi.org/10.1080/23723556.2017.1329692
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author Gupta, Amit
Anjomani-Virmouni, Sara
Koundouros, Nikos
Poulogiannis, George
author_facet Gupta, Amit
Anjomani-Virmouni, Sara
Koundouros, Nikos
Poulogiannis, George
author_sort Gupta, Amit
collection PubMed
description Cancer and Parkinson disease (PD) derive from distinct alterations in cellular processes, yet there are pathogenic mutations that are unequivocally linked to both diseases. Here we expand on our recent findings that loss of parkin RBR E3 ubiquitin protein ligase (PRKN, best known as PARK2)—which is genetically linked to PD—promotes cancer progression via redox-mediated inactivation of phosphatase and tensin homolog (PTEN) by S-nitrosylation.
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spelling pubmed-57069352018-05-19 PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN Gupta, Amit Anjomani-Virmouni, Sara Koundouros, Nikos Poulogiannis, George Mol Cell Oncol Author's View Cancer and Parkinson disease (PD) derive from distinct alterations in cellular processes, yet there are pathogenic mutations that are unequivocally linked to both diseases. Here we expand on our recent findings that loss of parkin RBR E3 ubiquitin protein ligase (PRKN, best known as PARK2)—which is genetically linked to PD—promotes cancer progression via redox-mediated inactivation of phosphatase and tensin homolog (PTEN) by S-nitrosylation. Taylor & Francis 2017-05-19 /pmc/articles/PMC5706935/ /pubmed/29209642 http://dx.doi.org/10.1080/23723556.2017.1329692 Text en © 2017 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Author's View
Gupta, Amit
Anjomani-Virmouni, Sara
Koundouros, Nikos
Poulogiannis, George
PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title_full PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title_fullStr PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title_full_unstemmed PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title_short PARK2 loss promotes cancer progression via redox-mediated inactivation of PTEN
title_sort park2 loss promotes cancer progression via redox-mediated inactivation of pten
topic Author's View
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706935/
https://www.ncbi.nlm.nih.gov/pubmed/29209642
http://dx.doi.org/10.1080/23723556.2017.1329692
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