Evidence map›Paper›PMID 24108109›Full record

ReviewEndocrine-related cancer2013

The dual role of filamin A in cancer: can't live with (too much of) it, can't live without it.

Rosalinda M Savoy, Paramita M Ghosh

Open access · bronzeAbstract readReview
In one paragraph

Review in Endocrine-related cancer, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

106 citing papers in PubMed, 1 synthesis or guideline pooled it, 163 citations in OpenAlex.

  1. Biomarkers of tumor invasiveness in proteomics (Review).International journal of oncology · 2020
    Pooled it
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46 more citing papers are in PubMed but not listed here.

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.

Rosalinda M SavoyDepartment of Urology, University of California Davis School of Medicine, University of California, 4860 Y Street, Suite 3500, Sacramento, California 95817, USA VA Northern California Health Care System, Mather, California, USA.
Paramita M Ghosh
University of California, Davis · US

Funding

Rapamycin Regulation of the Androgen Receptor: Implications in Prostate CancerR01CA133209 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GHOSH, PARAMITA M. · 2009 to 2013
$1.1M
Loss of Filamin A Nuclear Localization in Prostate Cancer ProgressionI01BX000400 · VA · VA NORTHERN CALIFORNIA HEALTH CARE SYS · PI GHOSH, PARAMITA M. · 2011 to 2019
–
BLRD VA I01 BX000400NCI NIH HHS CA133209NCI NIH HHS R01 CA133209
6 · The paper itself

Abstract

Filamin A (FlnA) has been associated with actin as cytoskeleton regulator. Recently its role in the cell has come under scrutiny for FlnA's involvement in cancer development. FlnA was originally revealed as a cancer-promoting protein, involved in invasion and metastasis. However, recent studies have also found that under certain conditions, it prevented tumor formation or progression, confusing the precise function of FlnA in cancer development. Here, we try to decipher the role of FlnA in cancer and the implications for its dual role. We propose that differences in subcellular localization of FlnA dictate its role in cancer development. In the cytoplasm, FlnA functions in various growth signaling pathways, such as vascular endothelial growth factor, in addition to being involved in cell migration and adhesion pathways, such as R-Ras and integrin signaling. Involvement in these pathways and various others has shown a correlation between high cytoplasmic FlnA levels and invasive cancers. However, an active cleaved form of FlnA can localize to the nucleus rather than the cytoplasm and its interaction with transcription factors has been linked to a decrease in invasiveness of cancers. Therefore, overexpression of FlnA has a tumor-promoting effect, only when it is localized to the cytoplasm, whereas if FlnA undergoes proteolysis and the resulting C-terminal fragment localizes to the nucleus, it acts to suppress tumor growth and inhibit metastasis. Development of drugs to target FlnA and cause cleavage and subsequent localization to the nucleus could be a new and potent field of research in treating cancer.

Indexed as

CarcinogensAnimalsFilaminsHumansNeoplasmsSignal TransductionTumor Suppressor ProteinsCarcinogensFilaminsTumor Suppressor Proteinscancercytoplasmfilamin Alocalizationmetastasisnucleustranscription

Identifiers

PMID24108109
PMCPMC4376317
OpenAlexW2125348377

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.