Evidence map›Paper›PMID 10613913›Full record

ArticleThe Journal of cell biology1999

Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin.

M Cordenonsi, F D'Atri, E Hammar, D A Parry, J Kendrick-Jones, D Shore, S Citi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
10.5field-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

91 citing papers in PubMed, 302 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
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  8. Role ofCurrent developments in nutrition · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Serum Cingulin levels are increased in children with autism spectrum disorder.International journal of developmental disabilities · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Frontiers in molecular neuroscience · 2022
    Article
  20. Article

31 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

7 authors at 4 institutions in 4 countries.

M CordenonsiDepartment of Biology, University of Padova, 35121 Padova, Italy.
F D'Atri
E Hammar
D A Parry
J Kendrick-Jones
D Shore
S Citi
University of Geneva · CHMassey University · NZMRC Laboratory of Molecular Biology · GBUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We characterized the sequence and protein interactions of cingulin, an M(r) 140-160-kD phosphoprotein localized on the cytoplasmic surface of epithelial tight junctions (TJ). The derived amino acid sequence of a full-length Xenopus laevis cingulin cDNA shows globular head (residues 1-439) and tail (1,326-1,368) domains and a central alpha-helical rod domain (440-1,325). Sequence analysis, electron microscopy, and pull-down assays indicate that the cingulin rod is responsible for the formation of coiled-coil parallel dimers, which can further aggregate through intermolecular interactions. Pull-down assays from epithelial, insect cell, and reticulocyte lysates show that an NH(2)-terminal fragment of cingulin (1-378) interacts in vitro with ZO-1 (K(d) approximately 5 nM), ZO-2, ZO-3, myosin, and AF-6, but not with symplekin, and a COOH-terminal fragment (377-1,368) interacts with myosin and ZO-3. ZO-1 and ZO-2 immunoprecipitates contain cingulin, suggesting in vivo interactions. Full-length cingulin, but not NH(2)-terminal and COOH-terminal fragments, colocalizes with endogenous cingulin in transfected MDCK cells, indicating that sequences within both head and rod domains are required for TJ localization. We propose that cingulin is a functionally important component of TJ, linking the submembrane plaque domain of TJ to the actomyosin cytoskeleton.

Indexed as

Xenopus ProteinsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell LineCell NucleusChickensCytoplasmDogsKinesinsMembrane ProteinsMolecular Sequence DataMyosinsPeptide FragmentsPhosphoproteinsCarrier ProteinsCGN protein, XenopusKinesinsMembrane ProteinsMyosinsPeptide FragmentsPhosphoproteinsTJP1 protein, XenopusXenopus ProteinsZonula Occludens-1 ProteinZonula Occludens-2 ProteinZonula Occludens Proteins

Identifiers

PMID10613913
PMCPMC2174252
OpenAlexW2043249951

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.