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Palmitoylation as a Key Regulator of Ras Localization and Function
Ras proteins require membrane association for proper function. This process is tightly regulated by reversible palmitoylation that controls not only the distribution over different subcellular compartments but also Ras compartmentalization within membrane subdomains. As a result, there is a growing...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8010249/ https://www.ncbi.nlm.nih.gov/pubmed/33816563 http://dx.doi.org/10.3389/fmolb.2021.659861 |
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author | Busquets-Hernández, Carla Triola, Gemma |
author_facet | Busquets-Hernández, Carla Triola, Gemma |
author_sort | Busquets-Hernández, Carla |
collection | PubMed |
description | Ras proteins require membrane association for proper function. This process is tightly regulated by reversible palmitoylation that controls not only the distribution over different subcellular compartments but also Ras compartmentalization within membrane subdomains. As a result, there is a growing interest in protein palmitoylation and the enzymes that control this process. In this minireview, we discuss how palmitoylation affects the localization and function of Ras proteins. A better understanding of the regulatory mechanism controlling protein lipidation is expected to provide new insights into the functional role of these modifications and may ultimately lead to the development of novel therapeutic approaches. |
format | Online Article Text |
id | pubmed-8010249 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-80102492021-04-01 Palmitoylation as a Key Regulator of Ras Localization and Function Busquets-Hernández, Carla Triola, Gemma Front Mol Biosci Molecular Biosciences Ras proteins require membrane association for proper function. This process is tightly regulated by reversible palmitoylation that controls not only the distribution over different subcellular compartments but also Ras compartmentalization within membrane subdomains. As a result, there is a growing interest in protein palmitoylation and the enzymes that control this process. In this minireview, we discuss how palmitoylation affects the localization and function of Ras proteins. A better understanding of the regulatory mechanism controlling protein lipidation is expected to provide new insights into the functional role of these modifications and may ultimately lead to the development of novel therapeutic approaches. Frontiers Media S.A. 2021-03-17 /pmc/articles/PMC8010249/ /pubmed/33816563 http://dx.doi.org/10.3389/fmolb.2021.659861 Text en Copyright © 2021 Busquets-Hernández and Triola. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Busquets-Hernández, Carla Triola, Gemma Palmitoylation as a Key Regulator of Ras Localization and Function |
title | Palmitoylation as a Key Regulator of Ras Localization and Function |
title_full | Palmitoylation as a Key Regulator of Ras Localization and Function |
title_fullStr | Palmitoylation as a Key Regulator of Ras Localization and Function |
title_full_unstemmed | Palmitoylation as a Key Regulator of Ras Localization and Function |
title_short | Palmitoylation as a Key Regulator of Ras Localization and Function |
title_sort | palmitoylation as a key regulator of ras localization and function |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8010249/ https://www.ncbi.nlm.nih.gov/pubmed/33816563 http://dx.doi.org/10.3389/fmolb.2021.659861 |
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