Evidence map›Paper›PMID 7525601›Full record

ArticleThe Journal of cell biology1994

Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins.

P D Kouklis, E Hutton, E Fuchs

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 282 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Type 2 Inflammation Contributes to Skin Barrier Dysfunction in Atopic Dermatitis.JID innovations : skin science from molecules to population health · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. EnteropathogenicCellular and molecular gastroenterology and hepatology · 2018
    Article
  13. Epidermolytic Ichthyosis Sine Epidermolysis.The American Journal of dermatopathology · 2017
    Article
  14. New insights into interactions between the nucleotide-binding domain of CFTR and keratin 8.Protein science : a publication of the Protein Society · 2017
    Article
  15. Article
  16. Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017
    Review
  17. Article
  18. Article
  19. Review
  20. Review

15 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

3 authors at 1 institution in 1 country.

P D KouklisHoward Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.
E Hutton
E Fuchs
Howard Hughes Medical Institute · US

Funding

GENE EXPRESSION AND DIFFERENTIATION IN HUMAN EPIDERMISR37AR027883 · NIAMS · UNIVERSITY OF CHICAGO · PI ELAINE FUCHS · 1994 to 2026
$13.3M
GENE EXPRESSION &DIFFERENTIATION IN HUMAN EPIDERMISR01AR027883 · NIAMS · UNIVERSITY OF CHICAGO · PI FUCHS, ELAINE · 1986 to 2022
$7.6M
NIAMS NIH HHS AR27883
6 · The paper itself

Abstract

In epidermal cells, keratin intermediate filaments connect with desmosomes to form extensive cadherin-mediated cytoskeletal architectures. Desmoplakin (DPI), a desmosomal component lacking a transmembrane domain, has been implicated in this interaction, although most studies have been conducted with cells that contain few or no desmosomes, and efforts to demonstrate direct interactions between desmoplakin and intermediate filaments have not been successful. In this report, we explore the biochemical nature of the connections between keratin filaments and desmosomes in epidermal keratinocytes. We show that the carboxy terminal "tail" of DPI associates directly with the amino terminal "head" of type II epidermal keratins, including K1, K2, K5, and K6. We have engineered and purified recombinant K5 head and DPI tail, and we demonstrate direct interaction in vitro by solution-binding assays and by ligand blot assays. This marked association is not seen with simple epithelial type II keratins, vimentin, or with type I keratins, providing a possible explanation for the greater stability of the epidermal keratin filament architecture over that of other cell types. We have identified an 18-amino acid residue stretch in the K5 head that is conserved only among type II epidermal keratins and that appears to play some role in DPI tail binding. This finding might have important implications for understanding a recent point mutation found within this binding site in a family with a blistering skin disorder.

Indexed as

Amino Acid SequenceCell LineConserved SequenceCytoskeletal ProteinsDesmoplakinsDesmosomesElectrophoresis, Polyacrylamide GelGenomic LibraryHumansIntermediate FilamentsKeratinocytesKeratinsMolecular Sequence DataProtein BindingRecombinant ProteinsSequence Homology, Amino AcidCytoskeletal ProteinsDesmoplakinsDSP protein, humanKeratinsRecombinant Proteins

Identifiers

PMID7525601
PMCPMC2200061
OpenAlexW2104635208

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.