Evidence map›Paper›PMID 24367162›Full record

ArticleBreast cancer (Dove Medical Press)2009

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

Anna C Cunningham-Edmondson, Steven K Hanks

Open access · goldAbstract read
In one paragraph

Article in Breast cancer (Dove Medical Press), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  10. A truncated phosphorylated p130Cas substrate domain is sufficient to drive breast cancer growth and metastasis formation in vivo.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
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  15. Cas proteins: dodgy scaffolding in breast cancer.Breast cancer research : BCR · 2014
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Anna C Cunningham-EdmondsonDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA ; Department of Cellular Biology and Anatomy, Medical College of Georgia, Augusta, GA, USA.
Steven K HanksDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.
Vanderbilt University · US

Funding

Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
FUNCTIONAL STUDIES OF FOCAL ADHESION KINASER01GM049882 · NIGMS · VANDERBILT UNIVERSITY · PI HANKS, STEVEN K. · 1995 to 2010
$3.2M
NCI NIH HHS T32 CA119925NIGMS NIH HHS R01 GM049882
6 · The paper itself

Abstract

Elevated Src tyrosine kinase activity is commonly observed in breast cancer and likely contributes to neoplasia and malignancy. p130Cas ("Crk-associated substrate") 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 "substrate domain" (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.

Indexed as

adhesionBCAR1FAKintegrinsSrctyrosine phosphorylation

Identifiers

PMID24367162
PMCPMC3022348
OpenAlexW2003049181

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.