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Protein Lipidation by Palmitoylation and Myristoylation in Cancer

Posttranslational modification of proteins with lipid moieties is known as protein lipidation. The attachment of a lipid molecule to proteins endows distinct properties, which affect their hydrophobicity, structural stability, localization, trafficking between membrane compartments, and influences i...

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Detalles Bibliográficos
Autores principales: Fhu, Chee Wai, Ali, Azhar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8173174/
https://www.ncbi.nlm.nih.gov/pubmed/34095144
http://dx.doi.org/10.3389/fcell.2021.673647
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author Fhu, Chee Wai
Ali, Azhar
author_facet Fhu, Chee Wai
Ali, Azhar
author_sort Fhu, Chee Wai
collection PubMed
description Posttranslational modification of proteins with lipid moieties is known as protein lipidation. The attachment of a lipid molecule to proteins endows distinct properties, which affect their hydrophobicity, structural stability, localization, trafficking between membrane compartments, and influences its interaction with effectors. Lipids or lipid metabolites can serve as substrates for lipidation, and the availability of these lipid substrates are tightly regulated by cellular metabolism. Palmitoylation and myristoylation represent the two most common protein lipid modifications, and dysregulation of protein lipidation is strongly linked to various diseases such as metabolic syndromes and cancers. In this review, we present recent developments in our understanding on the roles of palmitoylation and myristoylation, and their significance in modulating cancer metabolism toward cancer initiation and progression.
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spelling pubmed-81731742021-06-04 Protein Lipidation by Palmitoylation and Myristoylation in Cancer Fhu, Chee Wai Ali, Azhar Front Cell Dev Biol Cell and Developmental Biology Posttranslational modification of proteins with lipid moieties is known as protein lipidation. The attachment of a lipid molecule to proteins endows distinct properties, which affect their hydrophobicity, structural stability, localization, trafficking between membrane compartments, and influences its interaction with effectors. Lipids or lipid metabolites can serve as substrates for lipidation, and the availability of these lipid substrates are tightly regulated by cellular metabolism. Palmitoylation and myristoylation represent the two most common protein lipid modifications, and dysregulation of protein lipidation is strongly linked to various diseases such as metabolic syndromes and cancers. In this review, we present recent developments in our understanding on the roles of palmitoylation and myristoylation, and their significance in modulating cancer metabolism toward cancer initiation and progression. Frontiers Media S.A. 2021-05-20 /pmc/articles/PMC8173174/ /pubmed/34095144 http://dx.doi.org/10.3389/fcell.2021.673647 Text en Copyright © 2021 Fhu and Ali. https://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 Cell and Developmental Biology
Fhu, Chee Wai
Ali, Azhar
Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title_full Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title_fullStr Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title_full_unstemmed Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title_short Protein Lipidation by Palmitoylation and Myristoylation in Cancer
title_sort protein lipidation by palmitoylation and myristoylation in cancer
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8173174/
https://www.ncbi.nlm.nih.gov/pubmed/34095144
http://dx.doi.org/10.3389/fcell.2021.673647
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