Evidence map›Paper›PMID 21628459›Full record

ArticleThe Journal of biological chemistry2011

Prenylated c17orf37 induces filopodia formation to promote cell migration and metastasis.

Subhamoy Dasgupta, Ian Cushman, Marilyne Kpetemey, Patrick J Casey, Jamboor K Vishwanatha

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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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

5 authors at 3 institutions in 2 countries.

Subhamoy DasguptaDepartment of Biomedical Sciences and Institute for Cancer Research, University of North Texas Health Science Center, Fort Worth, Texas 76107, USA.
Ian Cushman
Marilyne Kpetemey
Patrick J Casey
Jamboor K Vishwanatha
University of North Texas Health Science Center · USDuke Medical Center · USNational University of Singapore · SG

Funding

Visceral Fat & Lipid & Inflammatory Risk factors: Role of EthnicityP20MD001633 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI VISHWANATHA, JAMBOOR K. · 2005 to 2009
$7.1M
Triple Negative Breast Cancer: Novel Biomarkers and Therapeutic StrategiesP20MD006882 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI CARDARELLI, KATHRYN MARIE · 2012 to 2016
$5.8M
NIMHD NIH HHS MD 001633NIMHD NIH HHS P20 MD001633NIMHD NIH HHS P20 MD006882
6 · The paper itself

Abstract

Post-translational modification by covalent attachment of isoprenoid lipids (prenylation) regulates the functions and biological activities of several proteins implicated in the oncogenic transformation and metastatic progression of cancer. The largest group of prenylated proteins contains a CAAX motif at the C-terminal that serves as a substrate for a series of post-translational modifications that convert these otherwise hydrophilic proteins to lipidated proteins, thus facilitating membrane association. C17orf37 (chromosome 17 open reading frame 37), also known as C35/Rdx12/MGC14832, located in the 17q12 amplicon, is overexpressed in human cancer, and its expression correlates with the migratory and invasive phenotype of cancer cells. Here we show that C17orf37 contains a functional CAAX motif and is post-translationally modified by protein geranylgeranyltransferase-I (GGTase-I). Geranylgeranylation of C17orf37 at the CAAX motif facilitates association of the protein to the inner leaflet of plasma membrane, enhances migratory phenotype of cells by inducing increased filopodia formation, and potentiates directional migration. A prenylation-deficient mutant of C17orf37 is functionally inactive and fails to trigger dissemination of tail vein-injected cells in a mouse model of metastasis. These findings demonstrate that prenylation is required for the function of the C17orf37 protein in cancer cells and imply that the post-translational modification may functionally regulate metastatic progression of disease.

Indexed as

Cell MovementNeoplasm MetastasisProtein PrenylationAlkyl and Aryl TransferasesAmino Acid SequenceAnimalsCell Line, TumorCell MembraneHumansIntracellular Signaling Peptides and ProteinsIntracellular SpaceMiceMolecular Sequence DataNeoplasm InvasivenessNeoplasm ProteinsNIH 3T3 CellsAlkyl and Aryl Transferasesgeranylgeranyltransferase type-IIntracellular Signaling Peptides and ProteinsMIEN1 protein, humanNeoplasm Proteins

Identifiers

PMID21628459
PMCPMC3138290
OpenAlexW1999348976

What OpenQuestion holds

Textmetadata
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.