Evidence map›Paper›PMID 9571235›Full record

ArticleMolecular biology of the cell1998

Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells.

S Yamashiro, Y Yamakita, S Ono, F Matsumura

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

96 citing papers in PubMed, 263 citations in OpenAlex.

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36 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

4 authors at 1 institution in 1 country.

S YamashiroDepartment of Molecular Biology and Biochemistry, Rutgers University, Busch Campus, Piscataway, New Jersey 08855, USA.
Y Yamakita
S Ono
F Matsumura
Rutgers, The State University of New Jersey · US

Funding

MICROFILAMENT ORGANIZATION DURING MITOSIS AND CELL TRANSR37CA042742 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MATSUMURA, FUMIO · 1991 to 1999
–
NCI NIH HHS R37 CA042742NCI NIH HHS R37 CA-42742
6 · The paper itself

Abstract

Fascin is an actin-bundling protein that is found in membrane ruffles, microspikes, and stress fibers. The expression of fascin is greatly increased in many transformed cells, as well as in specialized normal cells including neuronal cells and antigen-presenting dendritic cells. A morphological characteristic common to these cells expressing high levels of fascin is the development of many membrane protrusions in which fascin is predominantly present. To examine whether fascin contributes to the alterations in microfilament organization at the cell periphery, we have expressed fascin in LLC-PK1 epithelial cells to levels as high as those found in transformed cells and in specialized normal cells. Expression of fascin results in large changes in morphology, the actin cytoskeleton, and cell motility: fascin-transfected cells form an increased number of longer and thicker microvilli on apical surfaces, extend lamellipodia-like structures at basolateral surfaces, and show disorganization of cell-cell contacts. Cell migration activity is increased by 8-17 times when assayed by modified Boyden chamber. Microinjection of a fascin protein into LLC-PK1 cells causes similar morphological alterations including the induction of lamellipodia at basolateral surfaces and formation of an increased number of microvilli on apical surfaces. Furthermore, microinjection of fascin into REF-52 cells, normal fibroblasts, induces the formation of many lamellipodia at all regions of cell periphery. These results together suggest that fascin is directly responsible for membrane protrusions through reorganization of the microfilament cytoskeleton at the cell periphery.

Indexed as

Trans-ActivatorsActin CytoskeletonActinsAnimalsbeta CateninCarrier ProteinsCell LineCell Line, TransformedCell MembraneCell MovementCytoskeletal ProteinsCytoskeletonEpithelial CellsGene ExpressionHeLa CellsHumansActinsbeta CateninCarrier ProteinsCTNNB1 protein, humanCtnnb1 protein, ratCytoskeletal ProteinsfascinMicrofilament ProteinsTrans-ActivatorsVinculin

Identifiers

PMID9571235
PMCPMC25324
OpenAlexW2136841975

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.