Evidence map›Paper›PMID 2500446›Full record

ArticleThe Journal of cell biology1989

Identification of two distinct functional domains on vinculin involved in its association with focal contacts.

R Bendori, D Salomon, B Geiger

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.9field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 75 citations in OpenAlex.

  1. Fluctuation of zonulin levels in bloodWorld journal of gastroenterology · 2017
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  16. The uvomorulin-anchorage protein alpha catenin is a vinculin homologue.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
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  19. Article
  20. Complete sequence of human vinculin and assignment of the gene to chromosome 10.Proceedings of the National Academy of Sciences of the United States of America · 1990
    Article
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.

R BendoriDepartment of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
D Salomon
B Geiger
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report here on the identification of two distinct functional domains on chicken vinculin molecule, which can, independently, mediate its interaction with focal contacts in living cells. These findings were obtained by immunofluorescent labeling of COS cells transfected with a series of chicken vinculin-specific cDNA constructs derived from clones cVin1 and cVin5 (Bendori, R., D. Salomon, and B. Geiger. 1987. EMBO [Eur. Mol. Biol. Organ.] J. 6:2897-2905). These included a chimeric construct consisting of 5' sequences of cVin1 attached to the complementary 3' region of cVin5, as well as several constructs of either cVin1 or cVin5 from which 3' or 5' sequences were deleted. We show here that the products of both cVin1 and cVin5, and of the cVin1/cVin5 chimera, readily associated with focal contacts in transfected COS cells. Furthermore, 78 and 45 kD NH2-terminal fragments encoded by a deleted cVin1 and the 78-kD COOH-terminal portion of vinculin encoded by cVin5 were capable of binding specifically to focal contact areas. In contrast 3'-deletion mutants prepared from clone cVin5 and a 5'-deletion mutant of cVin1, lacking both NH2- and COOH-terminal sequences, failed to associate with focal contacts in transfected cells. The loss of binding was accompanied by an overall disarray of the microfilament system. These results, together with previous in vitro binding studies, suggest that vinculin contains at least two independent sites for binding to focal contacts; the NH2-terminal domain may contain the talin binding site while the COOH-terminal domain may mediate vinculin-vinculin interaction. Moreover, the disruptive effect of the double-deleted molecule (lacking the two focal-contact binding sites) on the organization of actin suggests that a distinct region involved in the binding of vinculin to the microfilament system is present in the NH2-terminal 45-kD region of the molecule.

Indexed as

Cell AdhesionAnimalsCell LineCytoskeletal ProteinsDNADNA Mutational AnalysisFluorescent Antibody TechniqueGene Expression RegulationIntercellular JunctionsMolecular WeightMuscle ProteinsProtein ConformationTransfectionVinculinCytoskeletal ProteinsDNAMuscle ProteinsVinculin

Identifiers

PMID2500446
PMCPMC2115586
OpenAlexW1998238181

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.