A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs

While Janus-kinase (JAK)-inhibitors effectively reduce the inflammatory phenotype of myeloproliferative neoplasms (MPN), they do not affect disease burden or presence of the mutated clone to a major extent. Here, we show how Janus-kinase 2 (JAK2)-mutated cells persist through maintenance of the mito...

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Autores principales: Schnoeder, Tina M., Perner, Florian, Heidel, Florian H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2021
Materias:
Author Views
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8018336/
https://www.ncbi.nlm.nih.gov/pubmed/33855167
http://dx.doi.org/10.1080/23723556.2020.1871172
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author Schnoeder, Tina M.
Perner, Florian
Heidel, Florian H.
author_facet Schnoeder, Tina M.
Perner, Florian
Heidel, Florian H.
author_sort Schnoeder, Tina M.
collection PubMed
description While Janus-kinase (JAK)-inhibitors effectively reduce the inflammatory phenotype of myeloproliferative neoplasms (MPN), they do not affect disease burden or presence of the mutated clone to a major extent. Here, we show how Janus-kinase 2 (JAK2)-mutated cells persist through maintenance of the mitogen-activated protein kinase Interacting Serine/Threonine Kinase 1 (MKNK1) – Extracellular Signal-regulated Kinase (ERK)-axis by hijacking the splicing machinery through post-translational modifications.
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spelling pubmed-80183362021-04-13 A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs Schnoeder, Tina M. Perner, Florian Heidel, Florian H. Mol Cell Oncol Author Views While Janus-kinase (JAK)-inhibitors effectively reduce the inflammatory phenotype of myeloproliferative neoplasms (MPN), they do not affect disease burden or presence of the mutated clone to a major extent. Here, we show how Janus-kinase 2 (JAK2)-mutated cells persist through maintenance of the mitogen-activated protein kinase Interacting Serine/Threonine Kinase 1 (MKNK1) – Extracellular Signal-regulated Kinase (ERK)-axis by hijacking the splicing machinery through post-translational modifications. Taylor & Francis 2021-01-30 /pmc/articles/PMC8018336/ /pubmed/33855167 http://dx.doi.org/10.1080/23723556.2020.1871172 Text en © 2021 The Author(s). Published with license by Taylor & Francis Group, LLC. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Author Views
Schnoeder, Tina M.
Perner, Florian
Heidel, Florian H.
A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title_full A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title_fullStr A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title_full_unstemmed A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title_short A JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs
title_sort jak of all trades: how global phosphoproteomics reveal the achilles heel of mpns
topic Author Views
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8018336/
https://www.ncbi.nlm.nih.gov/pubmed/33855167
http://dx.doi.org/10.1080/23723556.2020.1871172
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