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Arresting kinase suppressor of Ras in an inactive state

Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of...

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Autores principales: Badshah, Syed Lal, Mabkhot, Yahia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5223383/
https://www.ncbi.nlm.nih.gov/pubmed/28069069
http://dx.doi.org/10.1186/s40880-017-0181-z
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author Badshah, Syed Lal
Mabkhot, Yahia
author_facet Badshah, Syed Lal
Mabkhot, Yahia
author_sort Badshah, Syed Lal
collection PubMed
description Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of Ras (KSR) protein using a small molecule as an inhibitor by Dhawan et al. A biphenyl ether analogue of a quinazoline binds in one of the binding pockets of KSR and results in stabilization of its inactive state. In this inactive state, KSR is unable to take part in the cascade of protein association to perform the signalling process.
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spelling pubmed-52233832017-01-11 Arresting kinase suppressor of Ras in an inactive state Badshah, Syed Lal Mabkhot, Yahia Chin J Cancer Editorial Ras protein signaling pathways are important in controlling the plight of different types of cancer. Here we discussed the paper entitled “Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling” published in Nature journal on inactivating the kinase suppressor of Ras (KSR) protein using a small molecule as an inhibitor by Dhawan et al. A biphenyl ether analogue of a quinazoline binds in one of the binding pockets of KSR and results in stabilization of its inactive state. In this inactive state, KSR is unable to take part in the cascade of protein association to perform the signalling process. BioMed Central 2017-01-09 /pmc/articles/PMC5223383/ /pubmed/28069069 http://dx.doi.org/10.1186/s40880-017-0181-z Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Editorial
Badshah, Syed Lal
Mabkhot, Yahia
Arresting kinase suppressor of Ras in an inactive state
title Arresting kinase suppressor of Ras in an inactive state
title_full Arresting kinase suppressor of Ras in an inactive state
title_fullStr Arresting kinase suppressor of Ras in an inactive state
title_full_unstemmed Arresting kinase suppressor of Ras in an inactive state
title_short Arresting kinase suppressor of Ras in an inactive state
title_sort arresting kinase suppressor of ras in an inactive state
topic Editorial
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5223383/
https://www.ncbi.nlm.nih.gov/pubmed/28069069
http://dx.doi.org/10.1186/s40880-017-0181-z
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