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Citrullination and the protein code: crosstalk between post-translational modifications in cancer

Post-translational modifications (PTMs) of proteins are central to epigenetic regulation and cellular signalling, playing an important role in the pathogenesis and progression of numerous diseases. Growing evidence indicates that protein arginine citrullination, catalysed by peptidylarginine deimina...

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Detalles Bibliográficos
Autores principales: Harada, Koyo, Carr, Simon M., Shrestha, Amit, La Thangue, Nicholas B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542456/
https://www.ncbi.nlm.nih.gov/pubmed/37778382
http://dx.doi.org/10.1098/rstb.2022.0243
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author Harada, Koyo
Carr, Simon M.
Shrestha, Amit
La Thangue, Nicholas B.
author_facet Harada, Koyo
Carr, Simon M.
Shrestha, Amit
La Thangue, Nicholas B.
author_sort Harada, Koyo
collection PubMed
description Post-translational modifications (PTMs) of proteins are central to epigenetic regulation and cellular signalling, playing an important role in the pathogenesis and progression of numerous diseases. Growing evidence indicates that protein arginine citrullination, catalysed by peptidylarginine deiminases (PADs), is involved in many aspects of molecular and cell biology and is emerging as a potential druggable target in multiple diseases including cancer. However, we are only just beginning to understand the molecular activities of PADs, and their underlying mechanistic details in vivo under both physiological and pathological conditions. Many questions still remain regarding the dynamic cellular functions of citrullination and its interplay with other types of PTMs. This review, therefore, discusses the known functions of PADs with a focus on cancer biology, highlighting the cross-talk between citrullination and other types of PTMs, and how this interplay regulates downstream biological events. This article is part of the Theo Murphy meeting issue ‘The virtues and vices of protein citrullination’.
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spelling pubmed-105424562023-10-03 Citrullination and the protein code: crosstalk between post-translational modifications in cancer Harada, Koyo Carr, Simon M. Shrestha, Amit La Thangue, Nicholas B. Philos Trans R Soc Lond B Biol Sci Articles Post-translational modifications (PTMs) of proteins are central to epigenetic regulation and cellular signalling, playing an important role in the pathogenesis and progression of numerous diseases. Growing evidence indicates that protein arginine citrullination, catalysed by peptidylarginine deiminases (PADs), is involved in many aspects of molecular and cell biology and is emerging as a potential druggable target in multiple diseases including cancer. However, we are only just beginning to understand the molecular activities of PADs, and their underlying mechanistic details in vivo under both physiological and pathological conditions. Many questions still remain regarding the dynamic cellular functions of citrullination and its interplay with other types of PTMs. This review, therefore, discusses the known functions of PADs with a focus on cancer biology, highlighting the cross-talk between citrullination and other types of PTMs, and how this interplay regulates downstream biological events. This article is part of the Theo Murphy meeting issue ‘The virtues and vices of protein citrullination’. The Royal Society 2023-11-20 2023-10-02 /pmc/articles/PMC10542456/ /pubmed/37778382 http://dx.doi.org/10.1098/rstb.2022.0243 Text en © 2023 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited.
spellingShingle Articles
Harada, Koyo
Carr, Simon M.
Shrestha, Amit
La Thangue, Nicholas B.
Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title_full Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title_fullStr Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title_full_unstemmed Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title_short Citrullination and the protein code: crosstalk between post-translational modifications in cancer
title_sort citrullination and the protein code: crosstalk between post-translational modifications in cancer
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542456/
https://www.ncbi.nlm.nih.gov/pubmed/37778382
http://dx.doi.org/10.1098/rstb.2022.0243
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