Evidence map›Paper›PMID 9382871›Full record

ArticleThe Journal of cell biology1997

Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily.

K N Pestonjamasp, R K Pope, J D Wulfkuhle, E J Luna

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Pooled it
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  16. Emerging roles for LPP in metastatic cancer progression.Journal of cell communication and signaling · 2018
    Review
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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

4 authors at 1 institution in 1 country.

K N PestonjamaspWorcester Foundation for Biomedical Research, University of Massachusetts Medical Center, Shrewsbury, Massachusetts 01545, USA.
R K Pope
J D Wulfkuhle
E J Luna
Foundation for Biomedical Research · US

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
CELL BIOLOGY OF DEVELOPMENTT32HD007312 · NICHD · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI RICHTER, JOEL D · 1985 to 2010
$1.9M
NICHD NIH HHS 5T32HD07312-12NICHD NIH HHS T32 HD007312NIGMS NIH HHS GM33048NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

Actin-binding membrane proteins are involved in both adhesive interactions and motile processes. We report here the purification and initial characterization of p205, a 205-kD protein from bovine neutrophil plasma membranes that binds to the sides of actin filaments in blot overlays. p205 is a tightly bound peripheral membrane protein that cosediments with endogenous actin in sucrose gradients and immunoprecipitates. Amino acid sequences were obtained from SDS-PAGE-purified p205 and used to generate antipeptide antibodies, immunolocalization data, and cDNA sequence information. The intracellular localization of p205 in MDBK cells is a function of cell density and adherence state. In subconfluent cells, p205 is found in punctate spots along the plasma membrane and in the cytoplasm and nucleus; in adherent cells, p205 concentrates with E-cadherin at sites of lateral cell-cell contact. Upon EGTA-mediated cell dissociation, p205 is internalized with E-cadherin and F-actin as a component of adherens junctions "rings." At later times, p205 is observed in cytoplasmic punctae. The high abundance of p205 in neutrophils and suspension-grown HeLa cells, which lack adherens junctions, further suggests that this protein may play multiple roles during cell growth, adhesion, and motility. Molecular cloning of p205 cDNA reveals a bipartite structure. The COOH terminus exhibits a striking similarity to villin and gelsolin, particularly in regions known to bind F-actin. The NH2 terminus is novel, but contains four potential nuclear targeting signals. Because p205 is now the largest known member of the villin/gelsolin superfamily, we propose the name, "supervillin." We suggest that supervillin may be involved in actin filament assembly at adherens junctions and that it may play additional roles in other cellular compartments.

Indexed as

Multigene FamilyActin CytoskeletonActinsAmino Acid SequenceAnimalsCarrier ProteinsCattleCell FractionationCloning, MolecularDogsEpithelial CellsGelsolinIntercellular JunctionsKidneyMembrane ProteinsMicrofilament ProteinsActinsCarrier ProteinsGelsolinMembrane ProteinsMicrofilament ProteinsNuclear Localization Signalsvillin

Identifiers

PMID9382871
PMCPMC2140202
OpenAlexW2166779196

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.