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...

Descripción completa

Guardado en:
Detalles Bibliográficos
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:
R
Q
Acceso en línea:https://doaj.org/article/fefc02ab41c149a6bc560619b2306232
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:fefc02ab41c149a6bc560619b2306232
record_format dspace
spelling oai:doaj.org-article:fefc02ab41c149a6bc560619b23062322021-12-02T20:12:58ZPerturbation of BRMS1 interactome reveals pathways that impact metastasis.1932-620310.1371/journal.pone.0259128https://doaj.org/article/fefc02ab41c149a6bc560619b23062322021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0259128https://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, p e0259128 (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/fefc02ab41c149a6bc560619b2306232
work_keys_str_mv AT rosalynczimmermann perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT mihaelaesardiu perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT christaamanton perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT mdsayemmiah perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT charlesasbanks perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT markkadams perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT devinckoestler perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT douglasrhurst perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT mickdedmonds perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT michaelpwashburn perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
AT dannyrwelch perturbationofbrms1interactomerevealspathwaysthatimpactmetastasis
_version_ 1718374862997684224