p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells

Anna C Cunningham-Edmondson1,2, Steven K Hanks11Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA; 2Department of Cellular Biology and Anatomy, Medical College of Georgia, Augusta, GA, USAAbstract: Elevated Src tyrosine kinase activity is comm...

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Autores principales:	Anna C Cunningham-Edmondson, Steven K Hanks
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2009
Materias:	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
Acceso en línea:	https://doaj.org/article/5bcf7b4d79a54bf8ac44e71757d8a5bf
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spelling	oai:doaj.org-article:5bcf7b4d79a54bf8ac44e71757d8a5bf2021-12-02T03:00:08Zp130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells1179-1314https://doaj.org/article/5bcf7b4d79a54bf8ac44e71757d8a5bf2009-12-01T00:00:00Zhttp://www.dovepress.com/p130cas-substrate-domain-signaling-promotes-migration-invasion-and-sur-a3807https://doaj.org/toc/1179-1314Anna C Cunningham-Edmondson1,2, Steven K Hanks11Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA; 2Department of Cellular Biology and Anatomy, Medical College of Georgia, Augusta, GA, USAAbstract: Elevated Src tyrosine kinase activity is commonly observed in breast cancer and likely contributes to neoplasia and malignancy. p130Cas (&ldquo;Crk-associated substrate&rdquo;) is a major Src substrate found at the sites where integrins mediate cell adhesion to the extracellular matrix. Src phosphorylates multiple tyrosines in the p130Cas &ldquo;substrate domain&rdquo; (SD) and this signaling event has been implicated in the promotion of cell motility, primarily from studies on fibroblasts. In breast cancer, studies on p130Cas have focused on its role in conferring antiestrogen resistance to cells that express the estrogen receptor (ER+). However, little is known regarding the role of p130Cas in the more aggressive estrogen receptor negative (ER-) breast cancers for which there is a need for development of effective targeted therapies. We found high levels of p130Cas SD tyrosine phosphorylation to be a common characteristic of ER- breast cancer cell lines, with particularly high levels observed for the BT-549 cell line. Using RNA interference to knock down p130Cas expression in BT-549 cells, combined with rescue by WT p130Cas versus a signaling-deficient control, we provide evidence that p130Cas SD tyrosine phosphorylation is an important signaling event in the migration, invasion, proliferation, and survival of this ER- breast cancer cell line.Keywords: adhesion, BCAR1, integrins, Src, FAK, tyrosine phosphorylation Anna C Cunningham-EdmondsonSteven K HanksDove Medical PressarticleNeoplasms. Tumors. Oncology. Including cancer and carcinogensRC254-282ENBreast Cancer: Targets and Therapy, Vol 2009, Iss default, Pp 39-52 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
spellingShingle	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282 Anna C Cunningham-Edmondson Steven K Hanks p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
description	Anna C Cunningham-Edmondson1,2, Steven K Hanks11Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA; 2Department of Cellular Biology and Anatomy, Medical College of Georgia, Augusta, GA, USAAbstract: Elevated Src tyrosine kinase activity is commonly observed in breast cancer and likely contributes to neoplasia and malignancy. p130Cas (&ldquo;Crk-associated substrate&rdquo;) is a major Src substrate found at the sites where integrins mediate cell adhesion to the extracellular matrix. Src phosphorylates multiple tyrosines in the p130Cas &ldquo;substrate domain&rdquo; (SD) and this signaling event has been implicated in the promotion of cell motility, primarily from studies on fibroblasts. In breast cancer, studies on p130Cas have focused on its role in conferring antiestrogen resistance to cells that express the estrogen receptor (ER+). However, little is known regarding the role of p130Cas in the more aggressive estrogen receptor negative (ER-) breast cancers for which there is a need for development of effective targeted therapies. We found high levels of p130Cas SD tyrosine phosphorylation to be a common characteristic of ER- breast cancer cell lines, with particularly high levels observed for the BT-549 cell line. Using RNA interference to knock down p130Cas expression in BT-549 cells, combined with rescue by WT p130Cas versus a signaling-deficient control, we provide evidence that p130Cas SD tyrosine phosphorylation is an important signaling event in the migration, invasion, proliferation, and survival of this ER- breast cancer cell line.Keywords: adhesion, BCAR1, integrins, Src, FAK, tyrosine phosphorylation
format	article
author	Anna C Cunningham-Edmondson Steven K Hanks
author_facet	Anna C Cunningham-Edmondson Steven K Hanks
author_sort	Anna C Cunningham-Edmondson
title	p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
title_short	p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
title_full	p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
title_fullStr	p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
title_full_unstemmed	p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
title_sort	p130cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
publisher	Dove Medical Press
publishDate	2009
url	https://doaj.org/article/5bcf7b4d79a54bf8ac44e71757d8a5bf
work_keys_str_mv	AT annaccunninghamedmondson p130cassubstratedomainsignalingpromotesmigrationinvasionandsurvivalofestrogenreceptornegativebreastcancercells AT stevenkhanks p130cassubstratedomainsignalingpromotesmigrationinvasionandsurvivalofestrogenreceptornegativebreastcancercells
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p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells

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