Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3

<p></p><div> <p>Protein arginine methyltransferase 5 (PRMT5) activity is dysregulated in many aggressive cancers and its enhanced levels are associated with increased tumour growth and survival. However, the role of PRMT5 in breast cancer remains underexplored. In this study,...

Full description

Saved in:
Bibliographic Details
Main Author: Harshita Shailesh (14779408) (author)
Other Authors: Kodappully S. Siveen (4246150) (author), Saïd Sif (13616740) (author)
Published: 2023
Subjects:
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1864513566193745920
author Harshita Shailesh (14779408)
author2 Kodappully S. Siveen (4246150)
Saïd Sif (13616740)
author2_role author
author
author_facet Harshita Shailesh (14779408)
Kodappully S. Siveen (4246150)
Saïd Sif (13616740)
author_role author
dc.creator.none.fl_str_mv Harshita Shailesh (14779408)
Kodappully S. Siveen (4246150)
Saïd Sif (13616740)
dc.date.none.fl_str_mv 2023-03-15T11:17:52Z
dc.identifier.none.fl_str_mv 10.1111/jcmm.16260
dc.relation.none.fl_str_mv https://figshare.com/articles/journal_contribution/Protein_arginine_methyltransferase_5_PRMT5_activates_WNT_catenin_signalling_in_breast_cancer_cells_via_epigenetic_silencing_of_DKK1_and_DKK3/22258549
dc.rights.none.fl_str_mv CC BY 4.0
info:eu-repo/semantics/openAccess
dc.subject.none.fl_str_mv Biomedical and clinical sciences
Oncology and carcinogenesis
Cell Biology
Molecular Medicine
dc.title.none.fl_str_mv Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
dc.type.none.fl_str_mv Text
Journal contribution
info:eu-repo/semantics/publishedVersion
text
contribution to journal
description <p></p><div> <p>Protein arginine methyltransferase 5 (PRMT5) activity is dysregulated in many aggressive cancers and its enhanced levels are associated with increased tumour growth and survival. However, the role of PRMT5 in breast cancer remains underexplored. In this study, we show that PRMT5 is overexpressed in breast cancer cell lines, and that it promotes WNT/β-CATENIN proliferative signalling through epigenetic silencing of pathway antagonists, <i>DKK1</i> and <i>DKK3</i>, leading to enhanced expression of <i>c-MYC</i>, <i>CYCLIN D1</i> and <i>SURVIVIN</i>. Through chromatin immunoprecipitation (ChIP) studies, we found that PRMT5 binds to the promoter region of WNT antagonists, <i>DKK1</i> and <i>DKK3</i>, and induces symmetric methylation of H3R8 and H4R3 histones. Our findings also show that PRMT5 inhibition using a specific small molecule inhibitor, compound 5 (CMP5), reduces PRMT5 recruitment as well as methylation of H3R8 and H4R3 histones in the promoter regions of <i>DKK1</i> and <i>DKK3</i>, which consequently results in reduced expression <i>CYCLIN D1</i> and <i>SURVIVIN</i>. Furthermore, CMP5 treatment either alone or in combination with 5-Azacytidine and Trichostatin A restored expression of <i>DKK1</i> and <i>DKK3</i> in TNBCs. PRMT5 inhibition also altered the growth characteristics of breast cancer cells and induced their death. Collectively, these results show that PRMT5 controls breast cancer cell growth through epigenetic silencing of WNT/β-CATENIN pathway antagonists, DKK1 and DKK3, resulting in up-regulation of WNT/β-CATENIN proliferative signalling.</p> </div><p></p><h2>Other Information</h2> <p> Published in: Journal of Cellular and Molecular Medicine<br> License: <a href="http://creativecommons.org/licenses/by/4.0/" target="_blank">http://creativecommons.org/licenses/by/4.0/</a><br>See article on publisher's website: <a href="http://dx.doi.org/10.1111/jcmm.16260" target="_blank">http://dx.doi.org/10.1111/jcmm.16260</a></p>
eu_rights_str_mv openAccess
id Manara2_0c105fa1429d904837291bf9061c2c81
identifier_str_mv 10.1111/jcmm.16260
network_acronym_str Manara2
network_name_str Manara2
oai_identifier_str oai:figshare.com:article/22258549
publishDate 2023
repository.mail.fl_str_mv
repository.name.fl_str_mv
repository_id_str
rights_invalid_str_mv CC BY 4.0
spelling Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3Harshita Shailesh (14779408)Kodappully S. Siveen (4246150)Saïd Sif (13616740)Biomedical and clinical sciencesOncology and carcinogenesisCell BiologyMolecular Medicine<p></p><div> <p>Protein arginine methyltransferase 5 (PRMT5) activity is dysregulated in many aggressive cancers and its enhanced levels are associated with increased tumour growth and survival. However, the role of PRMT5 in breast cancer remains underexplored. In this study, we show that PRMT5 is overexpressed in breast cancer cell lines, and that it promotes WNT/β-CATENIN proliferative signalling through epigenetic silencing of pathway antagonists, <i>DKK1</i> and <i>DKK3</i>, leading to enhanced expression of <i>c-MYC</i>, <i>CYCLIN D1</i> and <i>SURVIVIN</i>. Through chromatin immunoprecipitation (ChIP) studies, we found that PRMT5 binds to the promoter region of WNT antagonists, <i>DKK1</i> and <i>DKK3</i>, and induces symmetric methylation of H3R8 and H4R3 histones. Our findings also show that PRMT5 inhibition using a specific small molecule inhibitor, compound 5 (CMP5), reduces PRMT5 recruitment as well as methylation of H3R8 and H4R3 histones in the promoter regions of <i>DKK1</i> and <i>DKK3</i>, which consequently results in reduced expression <i>CYCLIN D1</i> and <i>SURVIVIN</i>. Furthermore, CMP5 treatment either alone or in combination with 5-Azacytidine and Trichostatin A restored expression of <i>DKK1</i> and <i>DKK3</i> in TNBCs. PRMT5 inhibition also altered the growth characteristics of breast cancer cells and induced their death. Collectively, these results show that PRMT5 controls breast cancer cell growth through epigenetic silencing of WNT/β-CATENIN pathway antagonists, DKK1 and DKK3, resulting in up-regulation of WNT/β-CATENIN proliferative signalling.</p> </div><p></p><h2>Other Information</h2> <p> Published in: Journal of Cellular and Molecular Medicine<br> License: <a href="http://creativecommons.org/licenses/by/4.0/" target="_blank">http://creativecommons.org/licenses/by/4.0/</a><br>See article on publisher's website: <a href="http://dx.doi.org/10.1111/jcmm.16260" target="_blank">http://dx.doi.org/10.1111/jcmm.16260</a></p>2023-03-15T11:17:52ZTextJournal contributioninfo:eu-repo/semantics/publishedVersiontextcontribution to journal10.1111/jcmm.16260https://figshare.com/articles/journal_contribution/Protein_arginine_methyltransferase_5_PRMT5_activates_WNT_catenin_signalling_in_breast_cancer_cells_via_epigenetic_silencing_of_DKK1_and_DKK3/22258549CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/222585492023-03-15T11:17:52Z
spellingShingle Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
Harshita Shailesh (14779408)
Biomedical and clinical sciences
Oncology and carcinogenesis
Cell Biology
Molecular Medicine
status_str publishedVersion
title Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
title_full Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
title_fullStr Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
title_full_unstemmed Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
title_short Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
title_sort Protein arginine methyltransferase 5 (PRMT5) activates WNT/β‐catenin signalling in breast cancer cells via epigenetic silencing of DKK1 and DKK3
topic Biomedical and clinical sciences
Oncology and carcinogenesis
Cell Biology
Molecular Medicine