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Unconventional protein post-translational modifications: the helmsmen in breast cancer

Breast cancer is the most prevalent malignant tumor and a leading cause of mortality among females worldwide. The tumorigenesis and progression of breast cancer involve complex pathophysiological processes, which may be mediated by post-translational modifications (PTMs) of proteins, stimulated by v...

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Autores principales: Liu, Jiena, Wang, Qin, Kang, Yujuan, Xu, Shouping, Pang, Da
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8881842/
https://www.ncbi.nlm.nih.gov/pubmed/35216622
http://dx.doi.org/10.1186/s13578-022-00756-z
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author Liu, Jiena
Wang, Qin
Kang, Yujuan
Xu, Shouping
Pang, Da
author_facet Liu, Jiena
Wang, Qin
Kang, Yujuan
Xu, Shouping
Pang, Da
author_sort Liu, Jiena
collection PubMed
description Breast cancer is the most prevalent malignant tumor and a leading cause of mortality among females worldwide. The tumorigenesis and progression of breast cancer involve complex pathophysiological processes, which may be mediated by post-translational modifications (PTMs) of proteins, stimulated by various genes and signaling pathways. Studies into PTMs have long been dominated by the investigation of protein phosphorylation and histone epigenetic modifications. However, with great advances in proteomic techniques, several other PTMs, such as acetylation, glycosylation, sumoylation, methylation, ubiquitination, citrullination, and palmitoylation have been confirmed in breast cancer. Nevertheless, the mechanisms, effects, and inhibitors of these unconventional PTMs (particularly, the non-histone modifications other than phosphorylation) received comparatively little attention. Therefore, in this review, we illustrate the functions of these PTMs and highlight their impact on the oncogenesis and progression of breast cancer. Identification of novel potential therapeutic drugs targeting PTMs and development of biological markers for the detection of breast cancer would be significantly valuable for the efficient selection of therapeutic regimens and prediction of disease prognosis in patients with breast cancer. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13578-022-00756-z.
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spelling pubmed-88818422022-02-28 Unconventional protein post-translational modifications: the helmsmen in breast cancer Liu, Jiena Wang, Qin Kang, Yujuan Xu, Shouping Pang, Da Cell Biosci Review Breast cancer is the most prevalent malignant tumor and a leading cause of mortality among females worldwide. The tumorigenesis and progression of breast cancer involve complex pathophysiological processes, which may be mediated by post-translational modifications (PTMs) of proteins, stimulated by various genes and signaling pathways. Studies into PTMs have long been dominated by the investigation of protein phosphorylation and histone epigenetic modifications. However, with great advances in proteomic techniques, several other PTMs, such as acetylation, glycosylation, sumoylation, methylation, ubiquitination, citrullination, and palmitoylation have been confirmed in breast cancer. Nevertheless, the mechanisms, effects, and inhibitors of these unconventional PTMs (particularly, the non-histone modifications other than phosphorylation) received comparatively little attention. Therefore, in this review, we illustrate the functions of these PTMs and highlight their impact on the oncogenesis and progression of breast cancer. Identification of novel potential therapeutic drugs targeting PTMs and development of biological markers for the detection of breast cancer would be significantly valuable for the efficient selection of therapeutic regimens and prediction of disease prognosis in patients with breast cancer. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13578-022-00756-z. BioMed Central 2022-02-25 /pmc/articles/PMC8881842/ /pubmed/35216622 http://dx.doi.org/10.1186/s13578-022-00756-z Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Liu, Jiena
Wang, Qin
Kang, Yujuan
Xu, Shouping
Pang, Da
Unconventional protein post-translational modifications: the helmsmen in breast cancer
title Unconventional protein post-translational modifications: the helmsmen in breast cancer
title_full Unconventional protein post-translational modifications: the helmsmen in breast cancer
title_fullStr Unconventional protein post-translational modifications: the helmsmen in breast cancer
title_full_unstemmed Unconventional protein post-translational modifications: the helmsmen in breast cancer
title_short Unconventional protein post-translational modifications: the helmsmen in breast cancer
title_sort unconventional protein post-translational modifications: the helmsmen in breast cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8881842/
https://www.ncbi.nlm.nih.gov/pubmed/35216622
http://dx.doi.org/10.1186/s13578-022-00756-z
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