Evidence map›Paper›PMID 7568023›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex.

D L Rimm, E R Koslov, P Kebriaei, C D Cianci, J S Morrow

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 288 papers.

0numbers the graph read from it
0cells of the map it votes in
288citing papers in PubMed
16.9field-weighted citation impact, top 1% 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

288 citing papers in PubMed, 734 citations in OpenAlex.

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  8. Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  13. TheProceedings of the National Academy of Sciences of the United States of America · 2024
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228 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

5 authors at 1 institution in 1 country.

D L RimmDepartment of Pathology, Yale University School of Medicine, New Haven, CT 06510, USA.
E R Koslov
P Kebriaei
C D Cianci
J S Morrow
Yale University · US

Funding

Topographic Spectrin Assembly in the Renal Tubule CellR01DK043812 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1991 to 2007
$1.9M
STRUCTURE AND FUNCTION OF THE RENAL EPITHELIAL CELL MEMBRANE SKELETONP01DK038979 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1987 to 1998
–
NIDDK NIH HHS P01-DK38979NIDDK NIH HHS R01-DK43812
6 · The paper itself

Abstract

Calcium-dependent homotypic cell-cell adhesion, mediated by molecules such as E-cadherin, guides the establishment of classical epithelial cell polarity and contributes to the control of migration, growth, and differentiation. These actions involve additional proteins, including alpha- and beta-catenin (or plakoglobin) and p120, as well as linkage to the cortical actin cytoskeleton. The molecular basis for these interactions and their hierarchy of interaction remain controversial. We demonstrate a direct interaction between F-actin and alpha (E)-catenin, an activity not shared by either the cytoplasmic domain of E-cadherin or beta-catenin. Sedimentation assays and direct visualization by transmission electron microscopy reveal that alpha 1(E)-catenin binds and bundles F-actin in vitro with micromolar affinity at a catenin/G-actin monomer ratio of approximately 1:7 (mol/mol). Recombinant human beta-catenin can simultaneously bind to the alpha-catenin/actin complex but does not bind actin directly. Recombinant fragments encompassing the amino-terminal 228 residues of alpha 1(E)-catenin or the carboxyl-terminal 447 residues individually bind actin in cosedimentation assays with reduced affinity compared with the full-length protein, and neither fragment bundles actin. Except for similarities to vinculin, neither region contains sequences homologous to established actin-binding proteins. Collectively these data indicate that alpha 1 (E)-catenin is a novel actin-binding and -bundling protein and support a model in which alpha 1(E)-catenin is responsible for organizing and tethering actin filaments at the zones of E-cadherin-mediated cell-cell contact.

Indexed as

Intercellular JunctionsActinsalpha CateninAnimalsCell CompartmentationCells, CulturedCytoskeletal ProteinsDogsFluorescent Antibody TechniquePeptide FragmentsRecombinant ProteinsStructure-Activity RelationshipActinsalpha CateninCytoskeletal ProteinsPeptide FragmentsRecombinant Proteins

Identifiers

PMID7568023
PMCPMC41057
OpenAlexW2143646667

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.