Evidence map›Paper›PMID 29743635›Full record

ArticleScientific reports2018

Morphoregulatory functions of the RNA-binding motif protein 3 in cell spreading, polarity and migration.

J Pilotte, W Kiosses, S W Chan, H P Makarenkova, E Dupont-Versteegden, P W Vanderklish

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

J PilotteDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, United States.
W KiossesDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, United States.
S W ChanDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, United States.
H P MakarenkovaDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, United States.
E Dupont-VersteegdenDepartment of Rehabilitation Sciences, University of Kentucky, Lexington, KY, 40536, United States.
P W VanderklishDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, United States. pvanderk@scripps.edu.
Scripps Research Institute · USUniversity of Kentucky · US

Funding

Lacrimal Gland Repair Using Progenitor CellsR01EY026202 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI MAKARENKOVA, HELEN P. · 2016 to 2025
$5.2M
Circadian regulation of microRNA biogenesis and functionR01NS066053 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI VANDERKLISH, PETER W · 2009 to 2012
$1.7M
NEI NIH HHS R01 EY026202NINDS NIH HHS R01 NS066053
6 · The paper itself

Abstract

RNA-binding proteins are emerging as key regulators of transitions in cell morphology. The RNA-binding motif protein 3 (RBM3) is a cold-inducible RNA-binding protein with broadly relevant roles in cellular protection, and putative functions in cancer and development. Several findings suggest that RBM3 has morphoregulatory functions germane to its roles in these contexts. For example, RBM3 helps maintain the morphological integrity of cell protrusions during cell stress and disease. Moreover, it is highly expressed in migrating neurons of the developing brain and in cancer invadopodia, suggesting roles in migration. We here show that RBM3 regulates cell polarity, spreading and migration. RBM3 was present in spreading initiation centers, filopodia and blebs that formed during cell spreading in cell lines and primary myoblasts. Reducing RBM3 triggered exaggerated spreading, increased RhoA expression, and a loss of polarity that was rescued by Rho kinase inhibition and overexpression of CRMP2. High RBM3 expression enhanced the motility of cells migrating by a mesenchymal mode involving extension of long protrusions, whereas RBM3 knockdown slowed migration, greatly reducing the ability of cells to extend protrusions and impairing multiple processes that require directional migration. These data establish novel functions of RBM3 of potential significance to tissue repair, metastasis and development.

Indexed as

Cell MovementCell PolarityAnimalsCell LineHumansMiceMyoblastsNeoplasm MetastasisRNA-Binding ProteinsWound HealingRBM3 protein, humanRbm3 protein, mouseRNA-Binding Proteins

Identifiers

PMID29743635
PMCPMC5943363
OpenAlexW2806619984

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.