Perturbation of BRMS1 interactome reveals pathways that impact metastasis

Breast Cancer Metastasis Suppressor 1 (BRMS1) expression is associated with longer patient survival in multiple cancer types. Understanding BRMS1 functionality will provide insights into both mechanism of action and will enhance potential therapeutic development. In this study, we confirmed that the...

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Autores principales:	Rosalyn C. Zimmermann, Mihaela E. Sardiu, Christa A. Manton, Md. Sayem Miah, Charles A. S. Banks, Mark K. Adams, Devin C. Koestler, Douglas R. Hurst, Mick D. Edmonds, Michael P. Washburn, Danny R. Welch
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/66f4e69019a44e34bc00a4bed0277ef7
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spelling	oai:doaj.org-article:66f4e69019a44e34bc00a4bed0277ef72021-11-25T06:19:45ZPerturbation of BRMS1 interactome reveals pathways that impact metastasis1932-6203https://doaj.org/article/66f4e69019a44e34bc00a4bed0277ef72021-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8598058/?tool=EBIhttps://doaj.org/toc/1932-6203Breast Cancer Metastasis Suppressor 1 (BRMS1) expression is associated with longer patient survival in multiple cancer types. Understanding BRMS1 functionality will provide insights into both mechanism of action and will enhance potential therapeutic development. In this study, we confirmed that the C-terminus of BRMS1 is critical for metastasis suppression and hypothesized that critical protein interactions in this region would explain its function. Phosphorylation status at S237 regulates BRMS1 protein interactions related to a variety of biological processes, phenotypes [cell cycle (e.g., CDKN2A), DNA repair (e.g., BRCA1)], and metastasis [(e.g., TCF2 and POLE2)]. Presence of S237 also directly decreased MDA-MB-231 breast carcinoma migration in vitro and metastases in vivo. The results add significantly to our understanding of how BRMS1 interactions with Sin3/HDAC complexes regulate metastasis and expand insights into BRMS1’s molecular role, as they demonstrate BRMS1 C-terminus involvement in distinct protein-protein interactions.Rosalyn C. ZimmermannMihaela E. SardiuChrista A. MantonMd. Sayem MiahCharles A. S. BanksMark K. AdamsDevin C. KoestlerDouglas R. HurstMick D. EdmondsMichael P. WashburnDanny R. WelchPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rosalyn C. Zimmermann Mihaela E. Sardiu Christa A. Manton Md. Sayem Miah Charles A. S. Banks Mark K. Adams Devin C. Koestler Douglas R. Hurst Mick D. Edmonds Michael P. Washburn Danny R. Welch Perturbation of BRMS1 interactome reveals pathways that impact metastasis
description	Breast Cancer Metastasis Suppressor 1 (BRMS1) expression is associated with longer patient survival in multiple cancer types. Understanding BRMS1 functionality will provide insights into both mechanism of action and will enhance potential therapeutic development. In this study, we confirmed that the C-terminus of BRMS1 is critical for metastasis suppression and hypothesized that critical protein interactions in this region would explain its function. Phosphorylation status at S237 regulates BRMS1 protein interactions related to a variety of biological processes, phenotypes [cell cycle (e.g., CDKN2A), DNA repair (e.g., BRCA1)], and metastasis [(e.g., TCF2 and POLE2)]. Presence of S237 also directly decreased MDA-MB-231 breast carcinoma migration in vitro and metastases in vivo. The results add significantly to our understanding of how BRMS1 interactions with Sin3/HDAC complexes regulate metastasis and expand insights into BRMS1’s molecular role, as they demonstrate BRMS1 C-terminus involvement in distinct protein-protein interactions.
format	article
author	Rosalyn C. Zimmermann Mihaela E. Sardiu Christa A. Manton Md. Sayem Miah Charles A. S. Banks Mark K. Adams Devin C. Koestler Douglas R. Hurst Mick D. Edmonds Michael P. Washburn Danny R. Welch
author_facet	Rosalyn C. Zimmermann Mihaela E. Sardiu Christa A. Manton Md. Sayem Miah Charles A. S. Banks Mark K. Adams Devin C. Koestler Douglas R. Hurst Mick D. Edmonds Michael P. Washburn Danny R. Welch
author_sort	Rosalyn C. Zimmermann
title	Perturbation of BRMS1 interactome reveals pathways that impact metastasis
title_short	Perturbation of BRMS1 interactome reveals pathways that impact metastasis
title_full	Perturbation of BRMS1 interactome reveals pathways that impact metastasis
title_fullStr	Perturbation of BRMS1 interactome reveals pathways that impact metastasis
title_full_unstemmed	Perturbation of BRMS1 interactome reveals pathways that impact metastasis
title_sort	perturbation of brms1 interactome reveals pathways that impact metastasis
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/66f4e69019a44e34bc00a4bed0277ef7
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Perturbation of BRMS1 interactome reveals pathways that impact metastasis

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