Evidence map›Paper›PMID 25428984›Full record

ArticleMolecular biology of the cell2015

The formin FMNL3 assembles plasma membrane protrusions that participate in cell-cell adhesion.

Timothy J Gauvin, Lorna E Young, Henry N Higgs

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. 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
1.8field-weighted citation impact, top 16% 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, 40 citations in OpenAlex.

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  17. Changes in E-cadherin rigidity sensing regulate cell adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

3 authors at 1 institution in 1 country.

Timothy J GauvinDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Lorna E YoungDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Henry N HiggsDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 henry.higgs@dartmouth.edu.
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
Comparative molecular physiology of mammalian forminsR01GM069818 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2004 to 2017
$4.3M
Filopodia assembly by FMNL3: biochemical mechanism and cellular functionR01GM109965 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2015 to 2017
$1.1M
Live Cell Confocal Microscope for FRAP/PAS10RR024688 · NCRR · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 2009 to 2009
$500k
NCI NIH HHS P30 CA023108NCRR NIH HHS S10 RR024688NCRR NIH HHS S10RR024688NIGMS NIH HHS R01 GM069818NIGMS NIH HHS R01 GM109965
6 · The paper itself

Abstract

FMNL3 is a vertebrate-specific formin protein previously shown to play a role in angiogenesis and cell migration. Here we define the cellular localization of endogenous FMNL3, the dynamics of GFP-tagged FMNL3 during cell migration, and the effects of FMNL3 suppression in mammalian culture cells. The majority of FMNL3 localizes in a punctate pattern, with >95% of these puncta being indistinguishable from the plasma membrane by fluorescence microscopy. A small number of dynamic cytoplasmic FMNL3 patches also exist, which enrich near cell-cell contact sites and fuse with the plasma membrane at these sites. These cytoplasmic puncta appear to be part of larger membranes of endocytic origin. On the plasma membrane, FMNL3 enriches particularly in filopodia and membrane ruffles and at nascent cell-cell adhesions. FMNL3-containing filopodia occur both at the cell-substratum interface and at cell-cell contacts, with the latter being 10-fold more stable. FMNL3 suppression by siRNA has two major effects: decrease in filopodia and compromised cell-cell adhesion in cells migrating as a sheet. Overall our results suggest that FMNL3 functions in assembly of actin-based protrusions that are specialized for cell-cell adhesion.

Indexed as

ActinsAnimalsCell AdhesionCell MembraneForminsHumansMiceProteinsPseudopodiaRNA, Small InterferingActinsFMNL3 protein, humanFMNL3 protein, mouseForminsProteinsRNA, Small Interfering

Identifiers

PMID25428984
PMCPMC4310738
OpenAlexW2110998227

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.