Evidence map›Paper›PMID 9763423›Full record

ArticleThe Journal of cell biology1998

An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3.

Y Izumi, T Hirose, Y Tamai, S Hirai, Y Nagashima, T Fujimoto, Y Tabuse, K J Kemphues, S Ohno

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.

0numbers the graph read from it
0cells of the map it votes in
165citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

165 citing papers in PubMed, 505 citations in OpenAlex.

  1. Article
  2. Article
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  4. A PDZ-kinase allosteric relay mediates Par complex regulator exchange.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
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  7. TheProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Article
  10. The Roles of Par3, Par6, and aPKC Polarity Proteins in Normal Neurodevelopment and in Neurodegenerative and Neuropsychiatric Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Review
  11. Review
  12. Dual Function of Par3 in Tumorigenesis.Frontiers in oncology · 2022
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

105 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

9 authors at 4 institutions in 2 countries.

Y IzumiDepartment of Molecular Biology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.
T Hirose
Y Tamai
S Hirai
Y Nagashima
T Fujimoto
Y Tabuse
K J Kemphues
S Ohno
Yokohama City University · JPCornell University · USGunma University · JPNEC (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell polarity is fundamental to differentiation and function of most cells. Studies in mammalian epithelial cells have revealed that the establishment and maintenance of cell polarity depends upon cell adhesion, signaling networks, the cytoskeleton, and protein transport. Atypical protein kinase C (PKC) isotypes PKCzeta and PKClambda have been implicated in signaling through lipid metabolites including phosphatidylinositol 3-phosphates, but their physiological role remains elusive. In the present study we report the identification of a protein, ASIP (atypical PKC isotype-specific interacting protein), that binds to aPKCs, and show that it colocalizes with PKClambda to the cell junctional complex in cultured epithelial MDCKII cells and rat intestinal epithelia. In addition, immunoelectron microscopy revealed that ASIP localizes to tight junctions in intestinal epithelial cells. Furthermore, ASIP shows significant sequence similarity to Caenorhabditis elegans PAR-3. PAR-3 protein is localized to the anterior periphery of the one-cell embryo, and is required for the establishment of cell polarity in early embryos. ASIP and PAR-3 share three PDZ domains, and can both bind to aPKCs. Taken together, our results suggest a role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity. The evolutionary conservation of the protein complex and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.

Indexed as

Caenorhabditis elegans ProteinsCarrier ProteinsCell Adhesion Molecules3T3 CellsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCaenorhabditis elegansCell Cycle ProteinsCell LineCell PolarityDogsEpithelial CellsHelminth ProteinsIntestinal MucosaIsoenzymesAdaptor Proteins, Signal TransducingCaenorhabditis elegans ProteinsCarrier ProteinsCell Adhesion MoleculesCell Cycle ProteinsHelminth ProteinsIsoenzymesPAR-3 protein, C elegansPard3 protein, mouseProtein Kinase CProtein Kinase C-lambdaProtein Kinase C zetaProtein Serine-Threonine KinasesRecombinant ProteinsRNA, Messenger

Identifiers

PMID9763423
PMCPMC2132825
OpenAlexW2168436318

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.